메뉴 건너뛰기




Volumn 1827, Issue 8-9, 2013, Pages 892-913

Molecular mechanisms for generating transmembrane proton gradients

Author keywords

Bacterial reaction centers; Bacteriorhodopsin; Cytochrome c oxidase; Mn clusters; Photosystem II

Indexed keywords

AMINO ACID; BACTERIORHODOPSIN; MEMBRANE PROTEIN; OXYGEN; PROTON; PROTON PUMP; WATER; CYTOCHROME C OXIDASE;

EID: 84884313351     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2013.03.001     Document Type: Review
Times cited : (35)

References (366)
  • 1
    • 0347419305 scopus 로고    scopus 로고
    • The molecular machinery of Keilin's respiratory chain
    • P.R. Rich, The molecular machinery of Keilin's respiratory chain, Biochem. Soc. Trans. 31 (2003) 1095-1105. (Pubitemid 38030918)
    • (2003) Biochemical Society Transactions , vol.31 , Issue.6 , pp. 1095-1105
    • Rich, P.R.1
  • 2
    • 57049145761 scopus 로고    scopus 로고
    • A perspective on Peter Mitchell and the chemiosmotic theory
    • P.R. Rich, A perspective on Peter Mitchell and the chemiosmotic theory, J. Bioenerg. Biomembr. 40 (2008) 407-410.
    • (2008) J. Bioenerg. Biomembr , vol.40 , pp. 407-410
    • Rich, P.R.1
  • 3
    • 79951978630 scopus 로고    scopus 로고
    • Mitochondrial ion circuits
    • D.G. Nicholls, Mitochondrial ion circuits, Essays Biochem. 47 (2010) 25-35.
    • (2010) Essays Biochem , vol.47 , pp. 25-35
    • Nicholls, D.G.1
  • 5
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • DOI 10.1016/S0092-8674(03)00116-8
    • D.D. Newmeyer, S. Ferguson-Miller, Mitochondria: releasing power for life and unleashing the machineries of death, Cell 112 (2003) 481-490. (Pubitemid 36263081)
    • (2003) Cell , vol.112 , Issue.4 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 6
    • 33746349218 scopus 로고    scopus 로고
    • Energy transduction: Proton transfer through the respiratory complexes
    • DOI 10.1146/annurev.biochem.75.062003.101730
    • J.P.Hosler, S. Ferguson-Miller, D.A.Mills, Energy transduction: proton transfer through the respiratory complexes, Annu. Rev. Biochem. 75 (2006) 165-187. (Pubitemid 44118030)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 165-187
    • Hosler, J.P.1    Ferguson-Miller, S.2    Mills, D.A.3
  • 7
    • 57049180108 scopus 로고    scopus 로고
    • Cytochrome c oxidase: Exciting progress and remaining mysteries
    • P. Brzezinski, R. Gennis, Cytochrome c oxidase: exciting progress and remaining mysteries, J. Bioenerg. Biomembr. 40 (2008) 521-531.
    • (2008) J. Bioenerg. Biomembr , vol.40 , pp. 521-531
    • Brzezinski, P.1    Gennis, R.2
  • 8
    • 0036469776 scopus 로고    scopus 로고
    • Reaction centers: The structure and evolution of biological solar power
    • P. Heathcote, Reaction centers: the structure and evolution of biological solar power, Trends Biochem. Sci. 27 (2002) 79-86.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 79-86
    • Heathcote, P.1
  • 9
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • P. Mitchell, Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism, Nature 191 (1961) 144-148.
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 10
    • 0037333239 scopus 로고    scopus 로고
    • Rotary protein motors
    • DOI 10.1016/S0962-8924(03)00004-7
    • G. Oster, H. Wang, Rotary protein motors, Trends Cell Biol. 13 (2003) 114-121. (Pubitemid 36293783)
    • (2003) Trends in Cell Biology , vol.13 , Issue.3 , pp. 114-121
    • Oster, G.1    Wang, H.2
  • 11
    • 0242657369 scopus 로고    scopus 로고
    • Mechanics of coupling proton movements to c-ring rotation in ATP synthase
    • DOI 10.1016/S0014-5793(03)01101-3
    • R.H. Fillingame, C.M. Angevine, O.Y. Dmitriev, Mechanics of coupling proton movements to c-ring rotation in ATP synthase, FEBS Lett. 555 (2003) 29-34. (Pubitemid 37431092)
    • (2003) FEBS Letters , vol.555 , Issue.1 , pp. 29-34
    • Fillingame, R.H.1    Angevine, C.M.2    Dmitriev, O.Y.3
  • 12
    • 79957819196 scopus 로고    scopus 로고
    • Rotation and structure of FoF1-ATP synthase
    • D. Okuno, R. Iino, H. Noji, Rotation and structure of FoF1-ATP synthase, J. Biochem. 149 (2011) 655-664.
    • (2011) J. Biochem , vol.149 , pp. 655-664
    • Okuno, D.1    Iino, R.2    Noji, H.3
  • 14
    • 52649147435 scopus 로고    scopus 로고
    • Bacterial flagellar motor
    • Y. Sowa, R.M. Berry, Bacterial flagellar motor, Q. Rev. Biophys. 41 (2008) 103-132.
    • (2008) Q. Rev. Biophys , vol.41 , pp. 103-132
    • Sowa, Y.1    Berry, R.M.2
  • 15
    • 1242272754 scopus 로고    scopus 로고
    • Diversity of the mammalian sodium/proton exchanger SLC9 gene family
    • DOI 10.1007/s00424-003-1110-3, The ABCs of Solute Carriers: Physiological, Pathological and Therapeutic Implications of Human Membrane Transport Proteins
    • J. Orlowski, S. Grinstein, Diversity of the mammalian sodium/proton exchanger SLC9 gene family, Pflugers Arch. 447 (2004) 549-565. (Pubitemid 38241440)
    • (2004) Pflugers Archiv European Journal of Physiology , vol.447 , Issue.5 , pp. 549-565
    • Orlowski, J.1    Grinstein, S.2
  • 16
    • 59149095664 scopus 로고    scopus 로고
    • NhaA crystal structure: Functional- structural insights
    • E. Padan, L. Kozachkov, K. Herz, A. Rimon, NhaA crystal structure: functional- structural insights, J. Exp. Biol. 212 (2009) 1593-1603.
    • (2009) J. Exp. Biol , vol.212 , pp. 1593-1603
    • Padan, E.1    Kozachkov, L.2    Herz, K.3    Rimon, A.4
  • 17
    • 77953808359 scopus 로고    scopus 로고
    • CLC channels and transporters: Proteins with borderline personalities
    • A. Accardi, A. Picollo, CLC channels and transporters: proteins with borderline personalities, Biochim. Biophys. Acta 1798 (2010) 1457-1464.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1457-1464
    • Accardi, A.1    Picollo, A.2
  • 18
    • 0000058886 scopus 로고
    • Primary processes in bacterial photosynthesis: Structure and function of bacterial photosynthetic reaction centres
    • G. Feher, J.P. Allen, M.Y. Okamura, D.C. Rees, Primary processes in bacterial photosynthesis: structure and function of bacterial photosynthetic reaction centres, Nature 339 (1989) 111-116.
    • (1989) Nature , vol.339 , pp. 111-116
    • Feher, G.1    Allen, J.P.2    Okamura, M.Y.3    Rees, D.C.4
  • 19
    • 0000230806 scopus 로고
    • The reaction center protein from purple bacteria: Structure and function
    • M.R. Gunner, The reaction center protein from purple bacteria: structure and function, Curr. Top. Bioenerg. 16 (1991) 319-367.
    • (1991) Curr. Top. Bioenerg , vol.16 , pp. 319-367
    • Gunner, M.R.1
  • 20
    • 0242657390 scopus 로고    scopus 로고
    • Proton transfer pathways and mechanism in bacterial reaction centers
    • DOI 10.1016/S0014-5793(03)01149-9
    • M.L. Paddock, G. Feher,M.Y. Okamura, Proton transfer pathways andmechanismin bacterial reaction centers, FEBS Lett. 555 (2003) 45-50. (Pubitemid 37431095)
    • (2003) FEBS Letters , vol.555 , Issue.1 , pp. 45-50
    • Paddock, M.L.1    Feher, G.2    Okamura, M.Y.3
  • 22
    • 0036667743 scopus 로고    scopus 로고
    • Photosystem II: A multisubunit membrane protein that oxidises water
    • J. Barber, Photosystem II: a multisubunit membrane protein that oxidises water, Curr. Opin. Struct. Biol. 12 (2002) 523-530.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 523-530
    • Barber, J.1
  • 23
    • 0037295369 scopus 로고    scopus 로고
    • Photosystem II: The engine of life
    • DOI 10.1017/S0033583502003839
    • J. Barber, Photosystem II: the engine of life, Q. Rev. Biophys. 36 (2003) 71-89. (Pubitemid 36313960)
    • (2003) Quarterly Reviews of Biophysics , vol.36 , Issue.1 , pp. 71-89
    • Barber, J.1
  • 24
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II at 1.9 A resolution
    • Y.Umena, K. Kawakami, J.-R. Shen, N. Kamiya, Crystal structure of oxygen-evolving photosystem II at 1.9 A resolution, Nature 473 (2011) 55-60.
    • (2011) Nature , vol.473 , pp. 55-60
    • Umena, Y.1    Kawakami, K.2    Shen, J.-R.3    Kamiya, N.4
  • 25
    • 82755181814 scopus 로고    scopus 로고
    • Charge separation in photosystem II: A comparative and evolutionary overview
    • T. Cardona, A. Sedoud, N. Cox, A.W. Rutherford, Charge separation in photosystem II: a comparative and evolutionary overview, Biochim. Biophys. Acta 1817 (2012) 26-43.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 26-43
    • Cardona, T.1    Sedoud, A.2    Cox, N.3    Rutherford, A.W.4
  • 26
    • 84859631223 scopus 로고    scopus 로고
    • Recent developments in research on water oxidation by photosystem II
    • H. Dau, I. Zaharieva, M. Haumann, Recent developments in research on water oxidation by photosystem II, Curr. Opin. Chem. Biol. 16 (2012) 3-10.
    • (2012) Curr. Opin. Chem. Biol , vol.16 , pp. 3-10
    • Dau, H.1    Zaharieva, I.2    Haumann, M.3
  • 27
    • 0034734260 scopus 로고    scopus 로고
    • Protonation reactions and their coupling in bacteriorhodopsin
    • S.P. Balashov, Protonation reactions and their coupling in bacteriorhodopsin, Biochim. Biophys. Acta 1460 (2000) 75-94.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 75-94
    • Balashov, S.P.1
  • 28
    • 0034734246 scopus 로고    scopus 로고
    • Atomic resolution structures of bacteriorhodopsin photocycle intermediates: The role of descrete water molecules in the function of this lightdriven ion pump
    • H. Luecke, Atomic resolution structures of bacteriorhodopsin photocycle intermediates: the role of descrete water molecules in the function of this lightdriven ion pump, Biochim. Biophys. Acta 1460 (2000) 133-156.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 133-156
    • Luecke, H.1
  • 29
    • 0042386423 scopus 로고    scopus 로고
    • Proton affinity changes driving unidirectional proton transport in the bacteriorhodopsin photocycle
    • DOI 10.1016/S0022-2836(03)00903-3
    • A. Onufriev, A. Smondyrev, D. Bashford, Proton affinity changes driving unidirectional proton transport in the bacteriorhodopsin photocycle, J. Mol. Biol. 332 (2003) 1183-1193. (Pubitemid 37108810)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.5 , pp. 1183-1193
    • Onufriev, A.1    Smondyrev, A.2    Bashford, D.3
  • 30
    • 2442656919 scopus 로고    scopus 로고
    • Atomic resolution structures and the mechanism of ion pumping in bacteriorhodopsin
    • d1500-1993
    • B.W. Edmonds, H. Luecke, Atomic resolution structures and the mechanism of ion pumping in bacteriorhodopsin, Front. Biosci. 9 (2004) 1556-1566. (Pubitemid 38918614)
    • (2004) Frontiers in Bioscience , vol.9 , pp. 1556-1566
    • Edmonds, B.W.1    Luecke, H.2
  • 31
    • 33748903643 scopus 로고    scopus 로고
    • Proton transfers in the bacteriorhodopsin photocycle
    • DOI 10.1016/j.bbabio.2005.11.003, PII S0005272805002562
    • J.K. Lanyi, Proton transfers in the bacteriorhodopsin photocycle, Biochim. Biophys. Acta 1757 (2006) 1012-1018. (Pubitemid 44427748)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.8 , pp. 1012-1018
    • Lanyi, J.K.1
  • 32
    • 0017358508 scopus 로고
    • Proton pump coupled to cytochrome c oxidase in mitochondria
    • M.K. Wikstrom, Proton pump coupled to cytochrome c oxidase in mitochondria, Nature 266 (1977) 271-273. (Pubitemid 8071433)
    • (1977) Nature , vol.266 , Issue.5599 , pp. 271-273
    • Wikstrom, M.K.F.1
  • 33
    • 0028813330 scopus 로고
    • Towards an understanding of the chemistry of oxygen reduction and proton translocation in the iron-copper respiratory oxidases
    • P.R. Rich, Towards an understanding of the chemistry of oxygen reduction and proton translocation in the iron-copper respiratory oxidases, Aust. J. Plant Physiol. 22 (1995) 479-486.
    • (1995) Aust. J. Plant Physiol , vol.22 , pp. 479-486
    • Rich, P.R.1
  • 34
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper terminal oxidases
    • S. Ferguson-Miller, G.T. Babcock, Heme/copper terminal oxidases, Chem. Rev. 96 (1996) 2889-2907. (Pubitemid 126641120)
    • (1996) Chemical Reviews , vol.96 , Issue.7 , pp. 2889-2907
    • Ferguson-Miller, S.1    Babcock, G.T.2
  • 35
    • 81855190794 scopus 로고    scopus 로고
    • Energetics of direct and water-mediated proton-coupled electron transfer
    • V.R. Kaila, G. Hummer, Energetics of direct and water-mediated proton-coupled electron transfer, J. Am. Chem. Soc. 133 (2011) 19040-19043.
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 19040-19043
    • Kaila, V.R.1    Hummer, G.2
  • 36
    • 69549101850 scopus 로고    scopus 로고
    • Kinetic gating of the proton pump in cytochrome c oxidase
    • Y.C. Kim, M. Wikstrom, G. Hummer, Kinetic gating of the proton pump in cytochrome c oxidase, Proc. Natl. Acad. Sci. U. S. A. 106 (2009) 13707-13712.
    • (2009) Proc. Natl. Acad. Sci. U. S. A , vol.106 , pp. 13707-13712
    • Kim, Y.C.1    Wikstrom, M.2    Hummer, G.3
  • 37
    • 33749137961 scopus 로고    scopus 로고
    • Transmembrane proton translocation by cytochrome c oxidase
    • DOI 10.1016/j.bbabio.2006.05.020, PII S0005272806001472
    • G. Branden, R.B. Gennis, P. Brzezinski, Transmembrane proton translocation by cytochrome c oxidase, Biochim. Biophys. Acta 1757 (2006) 1052-1063. (Pubitemid 44467836)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.8 , pp. 1052-1063
    • Branden, G.1    Gennis, R.B.2    Brzezinski, P.3
  • 38
    • 34848850437 scopus 로고    scopus 로고
    • Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases
    • DOI 10.1016/j.bbabio.2007.06.008, PII S0005272807001533
    • M. Wikström, M.I. Verkhovsky, Mechanism and energetics of proton translocation by the respiratory heme-copper oxidases, Biochim. Biophys. Acta 1767 (2007) 1200-1214. (Pubitemid 47498307)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.10 , pp. 1200-1214
    • Wikstrom, M.1    Verkhovsky, M.I.2
  • 39
    • 84857923790 scopus 로고    scopus 로고
    • Cytochrome c oxidase: Intermediates of the catalytic cycle and their energy-coupled interconversion
    • A.A. Konstantinov, Cytochrome c oxidase: intermediates of the catalytic cycle and their energy-coupled interconversion, FEBS Lett. 586 (2012) 630-639.
    • (2012) FEBS Lett , vol.586 , pp. 630-639
    • Konstantinov, A.A.1
  • 41
    • 84857916726 scopus 로고    scopus 로고
    • Gating and regulation of the cytochrome c oxidase proton pump
    • S. Ferguson-Miller, C. Hiser, J. Liu, Gating and regulation of the cytochrome c oxidase proton pump, Biochim. Biophys. Acta 1817 (2012) 489-494.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 489-494
    • Ferguson-Miller, S.1    Hiser, C.2    Liu, J.3
  • 42
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respirations
    • G.T. Babcock, M. Wikström, Oxygen activation and the conservation of energy in cell respirations, Nature 356 (1992) 301-308.
    • (1992) Nature , vol.356 , pp. 301-308
    • Babcock, G.T.1    Wikström, M.2
  • 44
    • 0016754421 scopus 로고
    • The protonmotive Q cycle: A general formulation
    • P. Mitchell, The protonmotive Q cycle: a general formulation, FEBS Lett. 59 (1975) 137-139.
    • (1975) FEBS Lett , vol.59 , pp. 137-139
    • Mitchell, P.1
  • 45
    • 81155124280 scopus 로고    scopus 로고
    • Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. 1966
    • P. Mitchell, Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. 1966, Biochim. Biophys. Acta 1807 (2011) 1507-1538.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1507-1538
    • Mitchell, P.1
  • 46
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • P. Mitchell, Possible molecular mechanisms of the protonmotive function of cytochrome systems, J. Theor. Biol. 62 (1976) 327-367.
    • (1976) J. Theor. Biol , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 47
    • 2442609830 scopus 로고
    • Vectorial chemistry in bioenergetics: Cytochrome c oxidase as a redox linked proton pump
    • B.G. Malmstroem, Vectorial chemistry in bioenergetics: cytochrome c oxidase as a redox linked proton pump, Acc. Chem. Res. 26 (1993) 332-338.
    • (1993) Acc. Chem. Res , vol.26 , pp. 332-338
    • Malmstroem, B.G.1
  • 48
    • 33749184515 scopus 로고    scopus 로고
    • Electron tunneling chains of mitochondria
    • DOI 10.1016/j.bbabio.2006.04.015, PII S0005272806001083, Mitochondria: from Molecular Insight to Physiology and Pathology
    • C.C. Moser, T.A. Farid, S.E. Chobot, P.L. Dutton, Electron tunneling chains of mitochondria, Biochim. Biophys. Acta 1757 (2006) 1096-1109. (Pubitemid 44472548)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.9-10 , pp. 1096-1109
    • Moser, C.C.1    Farid, T.A.2    Chobot, S.E.3    Dutton, P.L.4
  • 49
    • 33745605230 scopus 로고    scopus 로고
    • Calculated proton uptake on anaerobic reduction of cytochrome c oxidase: Is the reaction electroneutral?
    • DOI 10.1021/bi052183d
    • Y. Song, E. Michonova-Alexova, M.R. Gunner, Calculated proton uptake on anaerobic reduction of cytochrome c oxidase: is the reaction electroneutral? Biochemistry 45 (2006) 7959-7975. (Pubitemid 43993218)
    • (2006) Biochemistry , vol.45 , Issue.26 , pp. 7959-7975
    • Song, Y.1    Michonova-Alexova, E.2    Gunner, M.R.3
  • 50
    • 77954762503 scopus 로고    scopus 로고
    • Electron flow through metalloproteins
    • H.B. Gray, J.R. Winkler, Electron flow through metalloproteins, Biochim. Biophys. Acta 1797 (2010) 1563-1572.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1563-1572
    • Gray, H.B.1    Winkler, J.R.2
  • 51
    • 0000178540 scopus 로고
    • The primary acceptor in bacterial photosynthesis: Obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas sphaeroides
    • M.Y. Okamura, R.A. Isaacson, G. Feher, The primary acceptor in bacterial photosynthesis: obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas sphaeroides, Proc. Natl. Acad. Sci. U. S. A. 72 (1975) 3492-3496.
    • (1975) Proc. Natl. Acad. Sci. U. S. A , vol.72 , pp. 3492-3496
    • Okamura, M.Y.1    Isaacson, R.A.2    Feher, G.3
  • 52
    • 33845374514 scopus 로고
    • Kinetic studies on the reaction center protein from Rhodopseudomonas sphaeroides: The temperature and free energy dependence of electron transfer between various quinones in the QA site and the oxidized bacteriochlorophyll dimer
    • M.R. Gunner, D.E. Robertson, P.L. Dutton, Kinetic studies on the reaction center protein from Rhodopseudomonas sphaeroides: the temperature and free energy dependence of electron transfer between various quinones in the QA site and the oxidized bacteriochlorophyll dimer, J. Phys. Chem. 90 (1986) 3783-3795.
    • (1986) J. Phys. Chem , vol.90 , pp. 3783-3795
    • Gunner, M.R.1    Robertson, D.E.2    Dutton, P.L.3
  • 54
    • 0032499644 scopus 로고    scopus 로고
    • A new metal-binding site in photosynthetic bacterial reaction centers that modulates Q(A) to Q(B) electron transfer
    • DOI 10.1021/bi980395n
    • L.M. Utschig, Y. Ohigashi, M.C. Thurnauer, D.M. Tiede, A new metal binding site in photosynthetic bacterial reaction centers that modulates QA to QB electron transfer, Biochemistry 37 (1998) 8278-8281. (Pubitemid 28275446)
    • (1998) Biochemistry , vol.37 , Issue.23 , pp. 8278-8281
    • Utschig, L.M.1    Ohigashi, Y.2    Thurnauer, M.C.3    Tiede, D.M.4
  • 56
    • 34249092919 scopus 로고    scopus 로고
    • Proton solvation and transport in aqueous and biomolecular systems: Insights from computer simulations
    • DOI 10.1021/jp070104x
    • J.M. Swanson, C.M. Maupin, H. Chen, M.K. Petersen, J. Xu, Y.Wu, G.A. Voth, Proton solvation and transport in aqueous and biomolecular systems: insights from computer simulations, J. Phys. Chem. B 111 (2007) 4300-4314. (Pubitemid 46787622)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.17 , pp. 4300-4314
    • Swanson, J.M.J.1    Maupin, C.M.2    Chen, H.3    Petersen, M.K.4    Xu, J.5    Wu, Y.6    Voth, G.A.7
  • 58
    • 0033461176 scopus 로고    scopus 로고
    • Conformationally controlled pK-switching in membrane proteins: One more mechanism specific to the enzyme catalysis?
    • DOI 10.1016/S0014-5793(99)01536-7, PII S0014579399015367
    • A.Y. Mulkidjanian, Conformationally controlled pK-switching in membrane proteins: one more mechanism specific to enzyme catalysis? FEBS Lett. 463 (1999) 199-204. (Pubitemid 30001919)
    • (1999) FEBS Letters , vol.463 , Issue.3 , pp. 199-204
    • Mulkidjanian, A.Y.1
  • 59
    • 0041471589 scopus 로고    scopus 로고
    • Calculation of proton transfers in bacteriorhodopsin bR and M intermediates
    • DOI 10.1021/bi034482d
    • Y. Song, J. Mao, M.R. Gunner, Calculation of proton transfers in bacteriorhodopsin bR and M intermediates, Biochemistry 42 (2003) 9875-9888. (Pubitemid 37012863)
    • (2003) Biochemistry , vol.42 , Issue.33 , pp. 9875-9888
    • Song, Y.1    Mao, J.2    Gunner, M.R.3
  • 60
    • 69249098842 scopus 로고    scopus 로고
    • Structural snapshots of conformational changes in a seven-helix membrane protein: Lessons from bacteriorhodopsin
    • T. Hirai, S. Subramaniam, J.K. Lanyi, Structural snapshots of conformational changes in a seven-helix membrane protein: lessons from bacteriorhodopsin, Curr. Opin. Struct. Biol. 19 (2009) 433-439.
    • (2009) Curr. Opin. Struct. Biol , vol.19 , pp. 433-439
    • Hirai, T.1    Subramaniam, S.2    Lanyi, J.K.3
  • 61
    • 0033614791 scopus 로고    scopus 로고
    • Calculated protein and proton motions coupled to electron transfer: Electron transfer from QA - To QB in bacterial photosynthetic reaction centers
    • E. Alexov, M.R. Gunner, Calculated protein and proton motions coupled to electron transfer: electron transfer from QA - to QB in bacterial photosynthetic reaction centers, Biochemistry 38 (1999) 8254-8270.
    • (1999) Biochemistry , vol.38 , pp. 8254-8270
    • Alexov, E.1    Gunner, M.R.2
  • 62
    • 0032947857 scopus 로고    scopus 로고
    • Transient accumulation of elastic energy in proton translocating ATP synthase
    • DOI 10.1016/S0014-5793(99)00386-5, PII S0014579399003865
    • D.A. Cherepanov, A.Y. Mulkidjanian, W. Junge, Transient accumulation of elastic energy in proton translocating ATP synthase, FEBS Lett. 449 (1999) 1-6. (Pubitemid 29182659)
    • (1999) FEBS Letters , vol.449 , Issue.1 , pp. 1-6
    • Cherepanov, D.A.1    Mulkidjanian, A.Y.2    Junge, W.3
  • 63
    • 56649116373 scopus 로고    scopus 로고
    • Ligand preference and orientation in b- and c-type heme-binding proteins
    • DOI 10.1002/prot.22097
    • C. Fufezan, J. Zhang, M.R. Gunner, Ligand preference and orientation in b- and c-type heme-binding proteins, Proteins 73 (2008) 690-704. (Pubitemid 352788650)
    • (2008) Proteins: Structure, Function and Genetics , vol.73 , Issue.3 , pp. 690-704
    • Fufezan, C.1    Zhang, J.2    Gunner, M.R.3
  • 64
    • 0041972670 scopus 로고    scopus 로고
    • How cytochromes with different folds control heme redox potentials
    • DOI 10.1021/bi027288k
    • J. Mao, K. Hauser, M.R. Gunner, How cytochromes with different folds control heme redox potentials, Biochemistry 42 (2003) 9829-9840. (Pubitemid 37012859)
    • (2003) Biochemistry , vol.42 , Issue.33 , pp. 9829-9840
    • Mao, J.1    Hauser, K.2    Gunner, M.R.3
  • 65
    • 2442488799 scopus 로고    scopus 로고
    • PH dependence of heme electrochemistry in cytochromes investigated by multiconformation continuum electrostatic calculations
    • DOI 10.1002/bip.20042
    • K. Hauser, J. Mao, M.R. Gunner, pH dependence of heme electrochemistry in cytochromes investigated by multiconformation continuum electrostatic calculations, Biopolymers 74 (2004) 51-54. (Pubitemid 38620616)
    • (2004) Biopolymers , vol.74 , Issue.1-2 , pp. 51-54
    • Hauser, K.1    Mao, J.2    Gunner, M.R.3
  • 66
    • 66149155473 scopus 로고    scopus 로고
    • Analysis of the electrochemistry of hemes with Ems spanning 800 mV
    • Z. Zheng, M.R. Gunner, Analysis of the electrochemistry of hemes with Ems spanning 800 mV, Proteins 75 (2009) 719-734.
    • (2009) Proteins , vol.75 , pp. 719-734
    • Zheng, Z.1    Gunner, M.R.2
  • 67
    • 77951156280 scopus 로고    scopus 로고
    • Understanding properties of cofactors in proteins: Redox potentials of synthetic cytochromes b
    • A.P. Gamiz-Hernandez, G. Kieseritzky, A.S. Galstyan, O. Demir-Kavuk, E.W. Knapp, Understanding properties of cofactors in proteins: redox potentials of synthetic cytochromes b, Chemphyschem 11 (2010) 1196-1206.
    • (2010) Chemphyschem , vol.11 , pp. 1196-1206
    • Gamiz-Hernandez, A.P.1    Kieseritzky, G.2    Galstyan, A.S.3    Demir-Kavuk, O.4    Knapp, E.W.5
  • 68
    • 79957992397 scopus 로고    scopus 로고
    • Proton-coupled electron transfer reactions at a hemepropionate in an iron-protoporphyrin-IX model compound
    • J.J. Warren, J.M. Mayer, Proton-coupled electron transfer reactions at a hemepropionate in an iron-protoporphyrin-IX model compound, J. Am. Chem. Soc. 133 (2011) 8544-8551.
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 8544-8551
    • Warren, J.J.1    Mayer, J.M.2
  • 69
    • 0001298277 scopus 로고
    • Solvation of anion radicals: Gas-phase versus solution
    • H. Shalev, D.H. Evans, Solvation of anion radicals: gas-phase versus solution, J. Am. Chem. Soc. 111 (1989) 2667-2674.
    • (1989) J. Am. Chem. Soc , vol.111 , pp. 2667-2674
    • Shalev, H.1    Evans, D.H.2
  • 70
    • 0347833201 scopus 로고    scopus 로고
    • Solvent dependence of the one-electron reduction of substituted benzo- and naphthoquinones
    • J.E. Heffner, C.T. Wigal, O.A. Moe, Solvent dependence of the one-electron reduction of substituted benzo-and napthoquinones, Electroanalysis 9 (1997) 629-632. (Pubitemid 127441285)
    • (1997) Electroanalysis , vol.9 , Issue.8 , pp. 629-632
    • Heffner, J.E.1    Wigal, C.T.2    Moe, O.A.3
  • 71
    • 0347749165 scopus 로고    scopus 로고
    • Using cyclic voltammetry and molecular modeling to determine substituent effects in the one-electron reduction of benzoquinones
    • J.E. Heffner, J.C. Raber, O.A. Moe Jr., C.T. Wigal, Using cyclic voltammetry and molecular modeling to determine substituent effects in the one-electron reduction of benzoquinones, J. Chem. Educ. 75 (1998) 365.
    • (1998) J. Chem. Educ , vol.75 , pp. 365
    • Heffner, J.E.1    Raber, J.C.2    Moe Jr., O.A.3    Wigal, C.T.4
  • 73
    • 0034640465 scopus 로고    scopus 로고
    • A pragmatic approach to structure based calculation of coupled proton and electron transfer in proteins
    • DOI 10.1016/S0005-2728(00)00060-8, PII S0005272800000608
    • M.R. Gunner, E. Alexov, A pragmatic approach to structure based calculation of coupled proton and electron transfer in proteins, Biochim. Biophys. Acta 1458 (2000) 63-87. (Pubitemid 30254251)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1458 , Issue.1 , pp. 63-87
    • Gunner, M.R.1    Alexov, E.2
  • 74
    • 2442693239 scopus 로고    scopus 로고
    • Macroscopic electrostatic models for protonation states in proteins
    • d1000-1499
    • D. Bashford, Macroscopic electrostatic models for protonation states in proteins, Front. Biosci. 9 (2004) 1082-1099. (Pubitemid 39060831)
    • (2004) Frontiers in Bioscience , vol.9 , pp. 1082-1099
    • Bashford, D.1
  • 75
    • 1542320003 scopus 로고    scopus 로고
    • Structural Interpretation of pH and Salt-Dependent Processes in Proteins with Computational Methods
    • DOI 10.1016/S0076-6879(04)80002-8
    • E.B. Garcia-Moreno, C.A. Fitch, Structural interpretation of pH and salt-dependent processes in proteins with computational methods, Methods Enzymol. 380 (2004) 20-51. (Pubitemid 38297489)
    • (2004) Methods in Enzymology , vol.380 , pp. 20-51
    • Garcia-Moreno E, B.1    Fitch, C.A.2
  • 76
    • 33749189483 scopus 로고    scopus 로고
    • Factors influencing the energetics of electron and proton transfers in proteins. What can be learned from calculations
    • DOI 10.1016/j.bbabio.2006.06.005, PII S0005272806001861
    • M.R. Gunner, J. Mao, Y. Song, J. Kim, Factors influencing energetics of electron and proton transfers in proteins. What can be learned from calculations, Biochim. Biophys. Acta 1757 (2006) 942-968. (Pubitemid 44472483)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.8 , pp. 942-968
    • Gunner, M.R.1    Mao, J.2    Song, Y.3    Kim, J.4
  • 77
    • 81055156035 scopus 로고    scopus 로고
    • Simulating electrostatic energies in proteins: Perspectives and some recent studies of pKas
    • A. Warshel, A. Dryga, Simulating electrostatic energies in proteins: perspectives and some recent studies of pKas, redox, and other crucial functional properties, Proteins 79 (2011) 3469-3484.
    • (2011) Redox, and Other Crucial Functional Properties, Proteins , vol.79 , pp. 3469-3484
    • Warshel, A.1    Dryga, A.2
  • 79
    • 81055156704 scopus 로고    scopus 로고
    • The pKa cooperative: A collaborative effort to advance structure-based calculations of pKa values and electrostatic effects in proteins
    • J.E. Nielsen, M.R. Gunner, B.E. Garcia-Moreno, The pKa cooperative: a collaborative effort to advance structure-based calculations of pKa values and electrostatic effects in proteins, Proteins 79 (2011) 3249-3259.
    • (2011) Proteins , vol.79 , pp. 3249-3259
    • Nielsen, J.E.1    Gunner, M.R.2    Garcia-Moreno, B.E.3
  • 80
    • 80052769847 scopus 로고    scopus 로고
    • The medium reorganization energy for the charge transfer reactions in proteins
    • L.I. Krishtalik, The medium reorganization energy for the charge transfer reactions in proteins, Biochim. Biophys. Acta 1807 (2011) 1444-1456.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1444-1456
    • Krishtalik, L.I.1
  • 81
    • 84862907865 scopus 로고    scopus 로고
    • Challenges for density functional theory
    • A.J. Cohen, P. Mori-Sanchez, W. Yang, Challenges for density functional theory, Chem. Rev. 112 (2012) 289-320.
    • (2012) Chem. Rev , vol.112 , pp. 289-320
    • Cohen, A.J.1    Mori-Sanchez, P.2    Yang, W.3
  • 82
    • 78650084194 scopus 로고    scopus 로고
    • Quantum chemical studies of proton-coupled electron transfer in metalloenzymes
    • P.E. Siegbahn, M.R. Blomberg, Quantum chemical studies of proton-coupled electron transfer in metalloenzymes, Chem. Rev. 110 (2010) 7040-7061.
    • (2010) Chem. Rev , vol.110 , pp. 7040-7061
    • Siegbahn, P.E.1    Blomberg, M.R.2
  • 83
  • 84
    • 70349971100 scopus 로고    scopus 로고
    • Enzymatic catalysis: The emerging role of conceptual density functional theory
    • G. Roos, P. Geerlings, J. Messens, Enzymatic catalysis: the emerging role of conceptual density functional theory, J. Phys. Chem. B 113 (2009) 13465-13475.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 13465-13475
    • Roos, G.1    Geerlings, P.2    Messens, J.3
  • 86
    • 0001664118 scopus 로고    scopus 로고
    • A mixed quantum mechanics/molecular mechanics (QM/MM) method for large-scale modeling of chemistry in protein environments
    • R.B. Murphy, D.M. Philipp, R.A. Friesner, A mixed quantum mechanics/molecular mechanics (QM/MM) method for large-scale modeling of chemistry in protein environments, J. Comput. Chem. 21 (2000) 1442-1457.
    • (2000) J. Comput. Chem , vol.21 , pp. 1442-1457
    • Murphy, R.B.1    Philipp, D.M.2    Friesner, R.A.3
  • 87
    • 62149122220 scopus 로고    scopus 로고
    • Progress in ab initio QM/MM free-energy simulations of electrostatic energies in proteins: Accelerated QM/MM studies of pKa, redox reactions and solvation free energies
    • S.C. Kamerlin, M. Haranczyk, A. Warshel, Progress in ab initio QM/MM free-energy simulations of electrostatic energies in proteins: accelerated QM/MM studies of pKa, redox reactions and solvation free energies, J. Phys. Chem. B 113 (2009) 1253-1272.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 1253-1272
    • Kamerlin, S.C.1    Haranczyk, M.2    Warshel, A.3
  • 88
    • 65549148068 scopus 로고    scopus 로고
    • Density functional theory (DFT) and combined quantum mechanical/molecular mechanics (QM/MM) studies on the oxygen activation step in nitric oxide synthase enzymes
    • S.P. de Visser, Density functional theory (DFT) and combined quantum mechanical/molecular mechanics (QM/MM) studies on the oxygen activation step in nitric oxide synthase enzymes, Biochem. Soc. Trans. 37 (2009) 373-377.
    • (2009) Biochem. Soc. Trans , vol.37 , pp. 373-377
    • De Visser, S.P.1
  • 89
    • 34047191046 scopus 로고    scopus 로고
    • QM/MM studies of enzymes
    • DOI 10.1016/j.cbpa.2007.01.684, PII S136759310700021X
    • H.M. Senn, W. Thiel, QM/MM studies of enzymes, Curr. Opin. Chem. Biol. 11 (2007) 182-187. (Pubitemid 46528365)
    • (2007) Current Opinion in Chemical Biology , vol.11 , Issue.2 , pp. 182-187
    • Senn, H.M.1    Thiel, W.2
  • 91
    • 0036787760 scopus 로고    scopus 로고
    • Combining conformational flexibility and continuum electrostatics for calculating pKas in proteins
    • R.E. Georgescu, E.G. Alexov, M.R. Gunner, Combining conformational flexibility and continuum electrostatics for calculating pKas in proteins, Biophys. J. 83 (2002) 1731-1748.
    • (2002) Biophys. J , vol.83 , pp. 1731-1748
    • Georgescu, R.E.1    Alexov, E.G.2    Gunner, M.R.3
  • 92
    • 42449113368 scopus 로고    scopus 로고
    • A computation in proteins with pH adapted conformations
    • DOI 10.1002/prot.21820
    • G. Kieseritzky, E.-W. Knapp, Optimizing pKa computation in proteins with pH adapted conformations, Proteins 71 (2008) 1335-1348. (Pubitemid 351564056)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.3 , pp. 1335-1348
    • Kieseritzky, G.1    Knapp, E.-W.2
  • 93
    • 62749167980 scopus 로고    scopus 로고
    • MCCE2: Improving protein pKa calculations with extensive side chain rotamer sampling
    • Y. Song, J. Mao, M.R. Gunner, MCCE2: improving protein pKa calculations with extensive side chain rotamer sampling, J. Comput. Chem. 30 (2009) 2231-2247.
    • (2009) J. Comput. Chem , vol.30 , pp. 2231-2247
    • Song, Y.1    Mao, J.2    Gunner, M.R.3
  • 94
    • 28644438898 scopus 로고    scopus 로고
    • Continuum electrostatics of proteins: Experimental test with model solvents and the method of the proteins pK calculations
    • DOI 10.1016/j.chemphys.2005.04.013, PII S0301010405001527
    • L.I. Krishtalik, Continuum electrostatics of proteins: experimental test with model solvents and the method of the proteins pK calculations, J. Chem. Phys. 319 (2005) 316-329. (Pubitemid 41750498)
    • (2005) Chemical Physics , vol.319 , Issue.1-3 , pp. 316-329
    • Krishtalik, L.I.1
  • 95
    • 0030945495 scopus 로고    scopus 로고
    • Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties
    • E.G. Alexov, M.R. Gunner, Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties, Biophys. J. 72 (1997) 2075-2093. (Pubitemid 27184435)
    • (1997) Biophysical Journal , vol.72 , Issue.5 , pp. 2075-2093
    • Alexov, E.G.1    Gunner, M.R.2
  • 96
    • 0025197061 scopus 로고
    • PK(a)'s of ionizable groups in proteins: Atomic detail from a continuum electrostatic model
    • D. Bashford, M. Karplus, The pKas of ionizable groups in proteins: atomic detail from a continuum electrostatic model, Biochemistry 29 (1990) 10219-10225. (Pubitemid 20384527)
    • (1990) Biochemistry , vol.29 , Issue.44 , pp. 10219-10225
    • Bashford, D.1    Karplus, M.2
  • 97
    • 0026095641 scopus 로고
    • Protonation of interacting residues in a protein by a Monte Carlo method: Application to lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides
    • P. Beroza, D.R. Fredkin, M.Y. Okamura, G. Feher, Protonation of interacting residues in a protein by a Monte Carlo method: application to Lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides, Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 5804-5808. (Pubitemid 21914834)
    • (1991) Proceedings of the National Academy of Sciences of the United States of America , vol.88 , Issue.13 , pp. 5804-5808
    • Beroza, P.1    Fredkin, D.R.2    Okamura, M.Y.3    Feher, G.4
  • 99
    • 33747131772 scopus 로고    scopus 로고
    • Toward the accurate first-principles prediction of ionization equilibria in proteins
    • DOI 10.1021/bi060706r
    • J. Khandogin, C.L. Brooks III, Toward the accurate first-principles prediction of ionization equilibria in proteins, Biochemistry 45 (2006) 9363-9373. (Pubitemid 44223241)
    • (2006) Biochemistry , vol.45 , Issue.31 , pp. 9363-9373
    • Khandogin, J.1    Brooks III, C.L.2
  • 100
    • 77955582352 scopus 로고    scopus 로고
    • Predicting the acid/base behavior of proteins: A constant-pH Monte Carlo approach with generalized born solvent
    • A. Aleksandrov, S. Polydorides, G. Archontis, T. Simonson, Predicting the acid/base behavior of proteins: a constant-pH Monte Carlo approach with generalized born solvent, J. Phys. Chem. B 114 (2010) 10634-10648.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 10634-10648
    • Aleksandrov, A.1    Polydorides, S.2    Archontis, G.3    Simonson, T.4
  • 101
    • 81055155931 scopus 로고    scopus 로고
    • PH replica-exchange method based on discrete protonation states
    • S.G. Itoh, A. Damjanovic, B.R. Brooks, pH replica-exchange method based on discrete protonation states, Proteins 79 (2011) 3420-3436.
    • (2011) Proteins , vol.79 , pp. 3420-3436
    • Itoh, S.G.1    Damjanovic, A.2    Brooks, B.R.3
  • 102
    • 81055140448 scopus 로고    scopus 로고
    • Is the prediction of pKa values by constant-pH molecular dynamics being hindered by inherited problems?
    • M. Machuqueiro, A.M. Baptista, Is the prediction of pKa values by constant-pH molecular dynamics being hindered by inherited problems? Proteins 79 (2011) 3437-3447.
    • (2011) Proteins , vol.79 , pp. 3437-3447
    • Machuqueiro, M.1    Baptista, A.M.2
  • 105
    • 11844302809 scopus 로고    scopus 로고
    • Energetics of quinone-dependent electron and proton transfers in Rhodobacter sphaeroides photosynthetic reaction centers
    • DOI 10.1021/bi048348k
    • Z. Zhu, M.R. Gunner, Energetics of quinone-dependent electron and proton transfers in Rhodobacter sphaeroides photosynthetic reaction centers, Biochemistry 44 (2005) 82-96. (Pubitemid 40095709)
    • (2005) Biochemistry , vol.44 , Issue.1 , pp. 82-96
    • Zhu, Z.1    Gunner, M.R.2
  • 106
    • 0021476470 scopus 로고
    • Calculations of electrostatic interactions in biological systems and in solutions
    • A. Warshel, S.T. Russell, Calculations of electrostatic interactions in biological systems and in solutions, Q. Rev. Biophys. 17 (1984) 283-422.
    • (1984) Q. Rev. Biophys , vol.17 , pp. 283-422
    • Warshel, A.1    Russell, S.T.2
  • 107
    • 33749223814 scopus 로고
    • Reevaluation of the Born model of ion hydration
    • A.A. Rashin, B. Honig, Reevaluation of the Born model of ion hydration, J. Phys. Chem. 89 (1985) 5588-5593.
    • (1985) J. Phys. Chem , vol.89 , pp. 5588-5593
    • Rashin, A.A.1    Honig, B.2
  • 108
    • 0034091669 scopus 로고    scopus 로고
    • Backbone dipoles generate positive potentials in all proteins: Origins and implications of the effect
    • M.R. Gunner, M.A. Saleh, E. Cross, A. ud-Doula, M. Wise, Backbone dipoles generate positive potentials in all proteins: origins and implications of the effect, Biophys. J. 78 (2000) 1126-1144. (Pubitemid 30141542)
    • (2000) Biophysical Journal , vol.78 , Issue.3 , pp. 1126-1144
    • Gunner, M.R.1    Saleh, M.A.2    Cross, E.3    Ud-Doula, A.4    Wise, M.5
  • 109
    • 18144394277 scopus 로고    scopus 로고
    • Are acidic and basic groups in buried proteins predicted to be ionized?
    • DOI 10.1016/j.jmb.2005.03.051
    • J. Kim, J. Mao, M.R. Gunner, Are acidic and basic groups in buried proteins predicted to be ionized? J. Mol. Biol. 348 (2005) 1283-1298. (Pubitemid 40613020)
    • (2005) Journal of Molecular Biology , vol.348 , Issue.5 , pp. 1283-1298
    • Kim, J.1    Mao, J.2    Gunner, M.R.3
  • 110
    • 0018792314 scopus 로고
    • A mechanism for the reduction of cytochromes by quinols in solution and its relevance to biological electron transfer reactions
    • P.R. Rich, D.S. Bendall, A mechanism for the reduction of cytochromes by quinols in solution and its relevance to biological electron transfer reactions, FEBS Lett. 105 (1979) 189-194.
    • (1979) FEBS Lett , vol.105 , pp. 189-194
    • Rich, P.R.1    Bendall, D.S.2
  • 112
    • 1242347393 scopus 로고    scopus 로고
    • Proton and electron transfer in the acceptor quinone complex of bacterial photosynthetic reaction centers
    • C.A. Wraight, Proton and electron transfer in the acceptor quinone complex of bacterial photosynthetic reaction centers, Front. Biosci. 9 (2004) 309-327.
    • (2004) Front. Biosci , vol.9 , pp. 309-327
    • Wraight, C.A.1
  • 113
    • 0035498860 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1038/35102067
    • S. Berneche, B. Roux, Energetics of ion conduction through the K+ channel, Nature 414 (2001) 73-77. (Pubitemid 33041625)
    • (2001) Nature , vol.414 , Issue.6859 , pp. 73-77
    • Berneche, S.1    Roux, B.2
  • 114
    • 0010624785 scopus 로고    scopus 로고
    • The effect of protein relaxation on charge-charge interactions and dielectric constants of proteins
    • Y.Y. Sham, I.Muegge, A.Warshel, The effect of protein relaxation on charge- charge interactions and dielectric constant of proteins, Biophys. J. 74 (1998) 1744-1753. (Pubitemid 28157913)
    • (1998) Biophysical Journal , vol.74 , Issue.4 , pp. 1744-1753
    • Sham, Y.Y.1    Muegge, I.2    Warshel, A.3
  • 115
    • 81055157735 scopus 로고    scopus 로고
    • MCCE analysis of the pKas of introduced buried acids and bases in staphylococcal nuclease
    • M.R. Gunner, X. Zhu, M.C. Klein, MCCE analysis of the pKas of introduced buried acids and bases in staphylococcal nuclease, Proteins 79 (2011) 3306-3319.
    • (2011) Proteins , vol.79 , pp. 3306-3319
    • Gunner, M.R.1    Zhu, X.2    Klein, M.C.3
  • 117
    • 0022816745 scopus 로고
    • The dielectric constant of a folded protein
    • M.K. Gilson, B.H. Honig, The dielectric constant of a folded protein, Biopolymers 25 (1986) 2097-2119.
    • (1986) Biopolymers , vol.25 , pp. 2097-2119
    • Gilson, M.K.1    Honig, B.H.2
  • 118
    • 0037453371 scopus 로고    scopus 로고
    • PH-dependent redox potential: How to use it correctly in the activation energy analysis
    • DOI 10.1016/S0005-2728(03)00020-3
    • L.I. Krishtalik, pH-dependent redox potential: how to use it correctly in the activation energy analysis, Biochim. Biophys. Acta 1604 (2003) 13-21. (Pubitemid 36398472)
    • (2003) Biochimica et Biophysica Acta - Bioenergetics , vol.1604 , Issue.1 , pp. 13-21
    • Krishtalik, L.I.1
  • 119
    • 0028787627 scopus 로고
    • Electron and proton transfer to the quinones in bacterial photosyntheic reaction centers: Insight from combined approaches of molecular genetics and biophysics
    • P. Sebban, P. Maroti, D.K. Hanson, Electron and proton transfer to the quinones in bacterial photosyntheic reaction centers: insight from combined approaches of molecular genetics and biophysics, Biochimie 77 (1995) 677-694.
    • (1995) Biochimie , vol.77 , pp. 677-694
    • Sebban, P.1    Maroti, P.2    Hanson, D.K.3
  • 121
    • 0025885119 scopus 로고
    • Photosynthetic reaction centres: Variations on a common structural theme?
    • W. Nitschke, A.W. Rutherford, Photosynthetic reaction centers: variations on a common structural theme? Trends Biochem. Sci. 16 (1991) 241-245. (Pubitemid 121004444)
    • (1991) Trends in Biochemical Sciences , vol.16 , Issue.1 , pp. 241-245
    • Nitschke, W.1    Will Am Rutherford, A.2
  • 122
    • 0032582723 scopus 로고    scopus 로고
    • Photosynthetic reaction centers
    • DOI 10.1016/S0014-5793(98)01245-9, PII S0014579398012459
    • J.P. Allen, J.C. Williams, Photosynthetic reaction centers, FEBS Lett. 438 (1998) 5-9. (Pubitemid 28517825)
    • (1998) FEBS Letters , vol.438 , Issue.1-2 , pp. 5-9
    • Allen, J.P.1    Williams, J.C.2
  • 123
    • 0024726467 scopus 로고
    • Pathway of proton transfer in bacterial reaction centers: Replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover
    • M.L. Paddock, S.H. Rongey, G. Feher, M.Y. Okamura, Pathway of proton transfer in bacterial reaction centers: replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover, Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 6602-6606.
    • (1989) Proc. Natl. Acad. Sci. U. S. A , vol.86 , pp. 6602-6606
    • Paddock, M.L.1    Rongey, S.H.2    Feher, G.3    Okamura, M.Y.4
  • 124
    • 0039286908 scopus 로고
    • Electrostatic effects of replacing Asp-L210 with Asn in bacterial RCs from Rb sphaeroides
    • M.L. Paddock, A. Juth, G. Feher, M.Y. Okamura, Electrostatic effects of replacing Asp-L210 with Asn in bacterial RCs from Rb. sphaeroides, Biophys. J. 61 (1992) A153.
    • (1992) Biophys. J , vol.61
    • Paddock, M.L.1    Juth, A.2    Feher, G.3    Okamura, M.Y.4
  • 125
    • 0028009920 scopus 로고
    • Pathway of proton transfer in bacterial reaction centers: Role of aspartate-L213 in proton transfers associated with reduction of quinone to dihydroquinone
    • M.L. Paddock, S.H. Rongey, P.H. McPherson, A. Juth, G. Feher, M.Y. Okamura, Pathway of proton transfer in bacterial reaction centers: role of aspartate-L213 in proton transfers associated with reduction of quinone to dihydroquinone, Biochemistry 33 (1994) 734-745. (Pubitemid 24064112)
    • (1994) Biochemistry , vol.33 , Issue.3 , pp. 734-745
    • Paddock, M.L.1    Rongey, S.H.2    McPherson, P.H.3    Juth, A.4    Feher, G.5    Okamura, M.Y.6
  • 127
    • 0029007257 scopus 로고
    • Electrostatic dominoes: Long distance propagation of mutational effects in photosynthetic reaction centers of Rhodobacter capsulatus
    • P. Sebban, P. Maroti, M. Schiffer, D.K. Hanson, Electrostatic dominoes: long distance propagation of mutational effects in photosynthetic reaction centers of Rhodobacter capsulatus, Biochemistry 34 (1995) 8390-8397.
    • (1995) Biochemistry , vol.34 , pp. 8390-8397
    • Sebban, P.1    Maroti, P.2    Schiffer, M.3    Hanson, D.K.4
  • 128
    • 0025169243 scopus 로고
    • A crucial role for AspL213 in the proton transfer pathway to the secondary quinone of reaction centers from Rhodobacter sphaeroides
    • E. Takahashi, C.A. Wraight, A crucial role for AspL213 in the proton transfer pathway to the secondary quinone of reaction centers from Rhodobacter sphaeroides, Biochim. Biophys. Acta 1020 (1990) 107-111.
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 107-111
    • Takahashi, E.1    Wraight, C.A.2
  • 129
    • 0026502431 scopus 로고
    • Proton and electron transfer in the acceptor quinone complex of Rhodobacter sphaeroides reaction centers: Characterization of site-directed mutants of the two ionizable residues
    • E. Takahashi, C.A. Wraight, Proton and electron transfer in the acceptor quinone complex of Rhodobacter sphaeroides reaction centers: characterization of site-directed mutants of the two ionizable residues, Glu L212 and Asp L213, in the QB binding site, Biochemistry 31 (1992) 855-866.
    • (1992) Glu L212 and Asp L213, in the QB Binding Site, Biochemistry , vol.31 , pp. 855-866
    • Takahashi, E.1    Wraight, C.A.2
  • 130
    • 0037446648 scopus 로고    scopus 로고
    • Protein control of the redox potential of the primary quinone acceptor in reaction centers from Rhodobacter sphaeroides
    • T.A. Wells, E. Takahashi, C.A. Wraight, Protein control of the redox potential of the primary quinone acceptor in reaction centers from Rhodobacter sphaeroides, Biochemistry 42 (2003) 4064-4074.
    • (2003) Biochemistry , vol.42 , pp. 4064-4074
    • Wells, T.A.1    Takahashi, E.2    Wraight, C.A.3
  • 132
    • 0031719963 scopus 로고    scopus 로고
    • Calculation of protonation patterns in proteins with structural relaxation and molecular ensembles - Application to the photosynthetic reaction center
    • DOI 10.1007/s002490050174
    • B. Rabenstein, G.M. Ullmann, E.-W. Knapp, Calculation of protonation patterns in proteins with structural relaxation and molecular ensembles- application to the photosynthetic reaction center, Eur. Biophys. J. 27 (1998) 626-637. (Pubitemid 28446586)
    • (1998) European Biophysics Journal , vol.27 , Issue.6 , pp. 626-637
    • Rabenstein, B.1    Ullmann, G.M.2    Knapp, E.-W.3
  • 133
    • 0030030176 scopus 로고    scopus 로고
    • Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopseudomonas viridis
    • C.R.D. Lancaster, H. Michel, B. Honig, M.R. Gunner, Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopseudomonas viridis, Biophys. J. 70 (1996) 2469-2492. (Pubitemid 26000949)
    • (1996) Biophysical Journal , vol.70 , Issue.6 , pp. 2469-2492
    • Lancaster, C.R.D.1    Michel, H.2    Honig, B.3    Gunner, M.R.4
  • 134
    • 0034705023 scopus 로고    scopus 로고
    • - to Q(B) in photosynthetic reaction centers
    • DOI 10.1021/bi9929498
    • E. Alexov, J. Miksovska, L. Baciou, M. Schiffer, D.K. Hanson, P. Sebban, M.R. Gunner, Modeling the effects of mutations on the free energy of the first electron transfer from QA - to QB in photosynthetic reaction centers, Biochemistry 39 (2000) 5940-5952. (Pubitemid 30327067)
    • (2000) Biochemistry , vol.39 , Issue.20 , pp. 5940-5952
    • Alexov, E.1    Miksovska, J.2    Baciou, L.3    Schiffer, M.4    Hanson, D.K.5    Sebban, P.6    Gunner, M.R.7
  • 135
    • 0037426334 scopus 로고    scopus 로고
    • Redox potential of quinones in photosynthetic reaction centers from Rhodobacter sphaeroides: Dependence on protonation of Glu-L212 and Asp-L213
    • DOI 10.1021/bi026781t
    • H. Ishikita, G. Morra, E.W. Knapp, Redox potential of quinones in photosynthetic reaction centers from Rhodobacter sphaeroides: dependence on protonation of Glu-L212 and Asp-L213, Biochemistry 42 (2003) 3882-3892. (Pubitemid 36402681)
    • (2003) Biochemistry , vol.42 , Issue.13 , pp. 3882-3892
    • Ishikita, H.1    Morra, G.2    Knapp, E.-W.3
  • 136
    • 80055006037 scopus 로고    scopus 로고
    • Slow dissociation of a charged ligand: Analysis of the primary quinone (QA) site of photosynthetic bacterial reaction centers
    • J. Madeo, M. Mihajlovic, T. Lazaridis, M.R. Gunner, Slow dissociation of a charged ligand: analysis of the primary quinone (QA) site of photosynthetic bacterial reaction centers, J. Am. Chem. Soc. 133 (2011) 17375-17385.
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 17375-17385
    • Madeo, J.1    Mihajlovic, M.2    Lazaridis, T.3    Gunner, M.R.4
  • 138
    • 23944507024 scopus 로고    scopus 로고
    • A site in bacterial reaction centers
    • DOI 10.1021/bi050544j
    • J. Madeo, M.R. Gunner, Modeling binding kinetics at the QA site in bacterial reaction centers, Biochemistry 44 (2005) 10994-11004. (Pubitemid 41209036)
    • (2005) Biochemistry , vol.44 , Issue.33 , pp. 10994-11004
    • Madeo, J.1    Gunner, M.R.2
  • 139
    • 0002624919 scopus 로고
    • Quinone exchange in the QA binding site of photosystem II reaction center core preparations isolated from Chlamydomonas reinhardii
    • B.A. Diner, C. deVitry, J.-L. Popot, Quinone exchange in the QA binding site of photosystem II reaction center core preparations isolated from Chlamydomonas reinhardii, Biochim. Biophys. Acta 934 (1988) 47-54.
    • (1988) Biochim. Biophys. Acta , vol.934 , pp. 47-54
    • Diner, B.A.1    Devitry, C.2    Popot, J.-L.3
  • 140
    • 0001230179 scopus 로고
    • The iron-quinone electron-acceptor complex of photosystem II
    • B.A. Diner, V. Petrouleas, J.J. Wendoloski, The iron-quinone electron-acceptor complex of photosystem II, Physiol. Plant. 81 (1991) 423-436.
    • (1991) Physiol. Plant , vol.81 , pp. 423-436
    • Diner, B.A.1    Petrouleas, V.2    Wendoloski, J.J.3
  • 141
    • 0000029388 scopus 로고
    • The influence of the quinone-iron electron acceptor complex on the reaction centre photochemistry of photosystem II
    • F.J.E. van Mieghem, W. Nitschke, P. Mathis, A.W. Rutherford, The influence of the quinone-iron electron acceptor complex on the reaction centre photochemistry of photosystem II, Biochim. Biophys. Acta 977 (1989) 207-214.
    • (1989) Biochim. Biophys. Acta , vol.977 , pp. 207-214
    • Van Mieghem, F.J.E.1    Nitschke, W.2    Mathis, P.3    Rutherford, A.W.4
  • 142
    • 34250332693 scopus 로고    scopus 로고
    • Influence of the redox potential of the primary quinone electron acceptor on photoinhibition in photosystem II
    • DOI 10.1074/jbc.M610951200
    • C. Fufezan, C.M. Gross, M. Sjodin, A.W. Rutherford, A. Krieger-Liszkay, D. Kirilovsky, Influence of the redox potential of the primary quinone electron acceptor on photoinhibition in photosystem II, J. Biol. Chem. 282 (2007) 12492-12502. (Pubitemid 47100606)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 12492-12502
    • Fufezan, C.1    Gross, C.M.2    Sjodin, M.3    Rutherford, A.W.4    Krieger-Liszkay, A.5    Kirilovsky, D.6
  • 143
    • 84995002675 scopus 로고
    • The role of quinones in bacterial photosynthesis
    • C.A. Wraight, The role of quinones in bacterial photosynthesis, Photochem. Photobiol. 30 (1979) 767-776.
    • (1979) Photochem. Photobiol , vol.30 , pp. 767-776
    • Wraight, C.A.1
  • 144
    • 33845185134 scopus 로고
    • Temperature and -ΔG dependence of the electron transfer from BPh- to QA in reaction center protein from Rhodobacter sphaeroides with different quinones as QA
    • M.R. Gunner, P.L. Dutton, Temperature and -ΔG dependence of the electron transfer from BPh- to QA in reaction center protein from Rhodobacter sphaeroides with different quinones as QA, J. Am. Chem. Soc. 111 (1989) 3400-3412.
    • (1989) J. Am. Chem. Soc , vol.111 , pp. 3400-3412
    • Gunner, M.R.1    Dutton, P.L.2
  • 145
    • 0021741695 scopus 로고
    • Nanosecond fluorescence from isolated photosynthetic reaction centers of Rhodopseudomonas sphaeroides
    • DOI 10.1016/0005-2728(84)90205-6
    • N.W.T. Woodbury, W.W. Parson, Nanosecond fluorescence from isolated photosynthetic reaction centers from Rhodopseudomonas sphaeroides, Biochim. Biophys. Acta 767 (1984) 345-361. (Pubitemid 15218680)
    • (1984) Biochimica et Biophysica Acta - Bioenergetics , vol.767 , Issue.2 , pp. 345-361
    • Woodbury, N.W.T.1    Parson, W.W.2
  • 146
    • 0001334882 scopus 로고
    • Flash-induced H+ binding by bacterial photosynthetic reaction centers: Influences of the redox states of the acceptor quinones and primary donor
    • P. Maroti, C.A. Wraight, Flash-induced H+ binding by bacterial photosynthetic reaction centers: influences of the redox states of the acceptor quinones and primary donor, Biochim. Biophys. Acta 934 (1988) 329-347.
    • (1988) Biochim. Biophys. Acta , vol.934 , pp. 329-347
    • Maroti, P.1    Wraight, C.A.2
  • 147
    • 0021771802 scopus 로고
    • Electron transfer in reaction centers of Rhodopseudomonas sphaeroides: I. Determination of the charge recombination pathway of D+QAQB - And free energy and kinetic relations between QA -QB and QAQB - And f
    • D. Kleinfeld, M.Y. Okamura, G. Feher, Electron transfer in reaction centers of Rhodopseudomonas sphaeroides: I. Determination of the charge recombination pathway of D+QAQB - and free energy and kinetic relations between QA -QB and QAQB -, Biochim. Biophys. Acta 766 (1984) 126-140.
    • (1984) Biochim. Biophys. Acta , vol.766 , pp. 126-140
    • Kleinfeld, D.1    Okamura, M.Y.2    Feher, G.3
  • 148
    • 0028314473 scopus 로고
    • 2 in native and Glu-L212 to Gln mutant reaction centers from Rhodobacter sphaeroides
    • P.H. McPherson, M. Schonfeld, M.L. Paddock, M.Y. Okamura, G. Feher, Protonation and free energy changes associated with formation of QBH2 in native and Glu-L212 → Gln mutant reaction centers from Rhodobacter sphaeroides, Biochemistry 33 (1994) 1181-1193. (Pubitemid 24072448)
    • (1994) Biochemistry , vol.33 , Issue.5 , pp. 1181-1193
    • McPherson, P.H.1    Schonfeld, M.2    Paddock, M.L.3    Okamura, M.Y.4    Feher, G.5
  • 149
    • 50449087592 scopus 로고    scopus 로고
    • The redox midpoint potential of the primary quinone of reaction centers in chromatophores of Rhodobacter sphaeroides is pH independent
    • P. Maróti, C.A. Wraight, The redox midpoint potential of the primary quinone of reaction centers in chromatophores of Rhodobacter sphaeroides is pH independent, Eur. Biophys. J. 37 (2008) 1207-1217.
    • (2008) Eur. Biophys. J , vol.37 , pp. 1207-1217
    • Maróti, P.1    Wraight, C.A.2
  • 150
    • 0002735129 scopus 로고
    • Kinetics and thermodynamics of the P870 + QA- → P870 + QB- reaction in isolated reaction centers from the photosynthetic bacterium Rhodopseudomonas sphaeroides
    • L.J. Mancino, D.P. Dean, R.E. Blankenship, Kinetics and thermodynamics of the P870 + QA- → P870 + QB- reaction in isolated reaction centers from the photosynthetic bacterium Rhodopseudomonas sphaeroides, Biochim. Biophys. Acta 764 (1984) 46-54.
    • (1984) Biochim. Biophys. Acta , vol.764 , pp. 46-54
    • Mancino, L.J.1    Dean, D.P.2    Blankenship, R.E.3
  • 151
    • 0021674417 scopus 로고
    • Electron-transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: Evidence for light-induced structural changes
    • DOI 10.1021/bi00319a017
    • D. Kleinfeld, M.Y. Okamura, G. Feher, Electron-transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge separated state: evidence for light-induced structural changes, Biochemistry 23 (1984) 5780-5786. (Pubitemid 15189728)
    • (1984) Biochemistry , vol.23 , Issue.24 , pp. 5780-5786
    • Kleinfeld, D.1    Okamura, M.Y.2    Feher, G.3
  • 152
    • 0344193626 scopus 로고    scopus 로고
    • Electron transfer and protein dynamics in the photosynthetic reaction center
    • B.H. McMahon, J.D. Muller, C.A. Wraight, G.U. Nienhaus, Electron transfer and protein dynamics in the photosynthetic reaction center, Biophys. J. 74 (1998) 2567-2587. (Pubitemid 28225252)
    • (1998) Biophysical Journal , vol.74 , Issue.5 , pp. 2567-2587
    • McMahon, B.H.1    Muller, J.D.2    Wraight, C.A.3    Nienhaus, G.U.4
  • 153
    • 0037031293 scopus 로고    scopus 로고
    • B electron transfer in bacterial photosynthetic reaction centers: Effect of substrate position and tail length on the conformational gating step
    • DOI 10.1021/bi025573y
    • Q. Xu, L. Baciou, P. Sebban, M.R. Gunner, Exploring the energy landscape for QA - to QB electron transfer in bacterial photosynthetic reaction centers: effect of substrate position and tail length on the conformational gating step, Biochemistry 41 (2002) 10021-10025. (Pubitemid 34839748)
    • (2002) Biochemistry , vol.41 , Issue.31 , pp. 10021-10025
    • Xu, Q.1    Baciou, L.2    Sebban, P.3    Gunner, M.R.4
  • 154
    • 57049149598 scopus 로고    scopus 로고
    • Modification of quinone electrochemistry by the proteins in the biological electron transfer chains: Examples from photosynthetic reaction centers
    • M.R. Gunner, J. Madeo, Z. Zhu, Modification of quinone electrochemistry by the proteins in the biological electron transfer chains: examples from photosynthetic reaction centers, J. Bioenerg. Biomembr. 40 (2008) 509-519.
    • (2008) J. Bioenerg. Biomembr , vol.40 , pp. 509-519
    • Gunner, M.R.1    Madeo, J.2    Zhu, Z.3
  • 155
    • 0018725904 scopus 로고
    • Vectorial redox reactions of physiological quinones. II. A study of transient semiquinone formation
    • A. Futami, G. Hauska, Vectorial redox reactions of physiological quinones. II. A study of transient semiquinone formation, Biochim. Biophys. Acta 547 (1979) 597-608. (Pubitemid 10233773)
    • (1979) Biochimica et Biophysica Acta , vol.547 , Issue.3 , pp. 597-608
    • Futami, A.1    Hauska, G.2
  • 156
    • 0028877684 scopus 로고
    • Studies on a stabilisation of ubisemiquinone by Escherichia coli quinol oxidase
    • W.J. Ingledew, T. Ohnishi, J.C. Salerno, Studies on a stabilisation of ubisemiquinone by Escherichia coli quinol oxidase, cytochrome bo, Eur. J. Biochem. 227 (1995) 903-908.
    • (1995) Cytochrome Bo, Eur. J. Biochem , vol.227 , pp. 903-908
    • Ingledew, W.J.1    Ohnishi, T.2    Salerno, J.C.3
  • 157
    • 0038392248 scopus 로고    scopus 로고
    • Variation in proton donor/acceptor pathways in succinate: Quinone oxidoreductases
    • DOI 10.1016/S0014-5793(03)00390-9
    • G. Cecchini, E. Maklashina, V. Yankovskaya, T.M. Iverson, S. Iwata, Variation in proton donor/acceptor pathways in succinate:quinone oxidoreductases, FEBS Lett. 545 (2003) 31-38. (Pubitemid 36629633)
    • (2003) FEBS Letters , vol.545 , Issue.1 , pp. 31-38
    • Cecchini, G.1    Maklashina, E.2    Yankovskaya, V.3    Iverson, T.M.4    Iwata, S.5
  • 158
    • 0035979759 scopus 로고    scopus 로고
    • Succinate: Quinone oxidoreductases: What can we learn from Wolinella succinogenes quinol: Fumarate reductase?
    • C.R.D. Lancaster, Succinate: quinone oxidoreductases - what can we learn from Wolinella succinogenes quinol:fumarate reductase? FEBS Lett. 504 (2001) 133-141.
    • (2001) FEBS Lett , vol.504 , pp. 133-141
    • Lancaster, C.R.D.1
  • 160
    • 84864701195 scopus 로고    scopus 로고
    • EPR detection of two protein-associated ubiquinone components (SQ(Nf) and SQ(Ns)) in the membrane in situ and in proteoliposomes of isolated bovine heart complex i
    • T. Ohnishi, S.T. Ohnishi, K. Shinzawa-Itoh, S. Yoshikawa, R.T. Weber, EPR detection of two protein-associated ubiquinone components (SQ(Nf) and SQ(Ns)) in the membrane in situ and in proteoliposomes of isolated bovine heart complex I, Biochim. Biophys. Acta 1817 (2012) 1803-1809.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1803-1809
    • Ohnishi, T.1    Ohnishi, S.T.2    Shinzawa-Itoh, K.3    Yoshikawa, S.4    Weber, R.T.5
  • 161
    • 33646365537 scopus 로고    scopus 로고
    • Intraprotein proton transfer - Concepts and realities from the bacterial photosynthetic reaction center
    • M. Wikström (Ed.), Royal Society of Chemistry, Cambridge, U.K
    • C.A. Wraight, Intraprotein proton transfer - concepts and realities from the bacterial photosynthetic reaction center, in: M. Wikström (Ed.), Biophysical and Structural Aspects of Bioenergetics, Royal Society of Chemistry, Cambridge, U.K., 2005, pp. 273-313.
    • (2005) Biophysical and Structural Aspects of Bioenergetics , pp. 273-313
    • Wraight, C.A.1
  • 162
    • 0001011327 scopus 로고
    • Electrochemistry of ubiquinones, menaquinones and plastoquinones in aprotic solvents
    • R.C. Prince, P.L. Dutton, J.M. Bruce, Electrochemistry of ubiquinones, menaquinones and plastoquinones in aprotic solvents, FEBS Lett. 160 (1983) 273-276.
    • (1983) FEBS Lett , vol.160 , pp. 273-276
    • Prince, R.C.1    Dutton, P.L.2    Bruce, J.M.3
  • 163
    • 84975363015 scopus 로고
    • Proton effects in electrochemistry of quinone hydroquinone system in aprotic solvents
    • B.R. Eggins, J.Q. Chambers, Proton effects in electrochemistry of quinone hydroquinone system in aprotic solvents, J. Electrochem. Soc. 117 (1970) 186.
    • (1970) J. Electrochem. Soc , vol.117 , pp. 186
    • Eggins, B.R.1    Chambers, J.Q.2
  • 164
    • 0022404490 scopus 로고
    • 2-
    • DOI 10.1016/0005-2728(85)90179-3
    • D. Kleinfeld, M.Y. Okamura, G. Feher, Electron transfer in reaction centers of Rhodopseudomonas sphaeroides. II. Free energy and kinetic relations between the acceptor states QA -QB - and QAQB -2, Biochim. Biophys. Acta 809 (1985) 291-310. (Pubitemid 16240326)
    • (1985) Biochimica et Biophysica Acta - Bioenergetics , vol.809 , Issue.3 , pp. 291-310
    • Kleinfeld, D.1    Okamura, M.Y.2    Feher, G.3
  • 165
    • 0033621050 scopus 로고    scopus 로고
    • Observation of the protonated semiquinone intermediate in isolated reaction centers from Rhodobacter sphaeroides: Implications for the mechanism of electron and proton transfer in proteins
    • M.S. Graige, M.L. Paddock, G. Feher, M.Y. Okamura, Observation of the protonated semiquinone intermediate in isolated reaction centers from Rhodobacter sphaeroides: implications for the mechanism of electron and proton transfer in proteins, Biochemistry 38 (1999) 11465-11473.
    • (1999) Biochemistry , vol.38 , pp. 11465-11473
    • Graige, M.S.1    Paddock, M.L.2    Feher, G.3    Okamura, M.Y.4
  • 166
    • 0017392514 scopus 로고
    • Kinetics of electron transfer between the primary and the secondary electron acceptor in reaction centers from Rhodopseudomonas sphaeroides
    • A. Vermeglio, R.K. Clayton, Kinetics of electron transfer between the primary and secondary electron acceptor in reaction centers from Rhodoseudomonas sphaeroides, Biochim. Biophys. Acta 461 (1977) 159-165. (Pubitemid 8120610)
    • (1977) Biochimica et Biophysica Acta , vol.461 , Issue.1 , pp. 159-165
    • Vermeglio, A.1    Clayton, R.K.2
  • 167
    • 0000053485 scopus 로고
    • Immobilized radicals IV. Biological semiquinone anions and neutral semiquinones
    • B.J. Hales, E.E. Case, Immobilized radicals IV. Biological semiquinone anions and neutral semiquinones, Biochim. Biophys. Acta 637 (1981) 291-302.
    • (1981) Biochim. Biophys. Acta , vol.637 , pp. 291-302
    • Hales, B.J.1    Case, E.E.2
  • 169
    • 0029844155 scopus 로고    scopus 로고
    • Mechanism of proton-coupled electron transfer for quinone (Q(B) reduction in reaction centers of Rb. Sphaeroides
    • DOI 10.1021/ja960056m
    • M.S. Graige, M.L. Paddock, J.M. Bruce, G. Feher, M.Y. Okamura, Mechanism of proton-coupled electron transfer for quinone (QB) reduction in reaction centers of Rb. sphaeroides, J. Am. Chem. Soc. 118 (1996) 9005-9016. (Pubitemid 26342534)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.38 , pp. 9005-9016
    • Graige, M.S.1    Paddock, M.L.2    Bruce, J.M.3    Feher, G.4    Okamura, M.Y.5
  • 170
    • 0032562210 scopus 로고    scopus 로고
    • Energetics of electron-transfer and protonation reactions of the quinones in the photosynthetic reaction center of Rhodopseudomonas viridis
    • DOI 10.1021/bi971921y
    • B. Rabenstein, G.M. Ullmann, E.-W. Knapp, Energetics of electron-transfer and protonation reactions of the quinones in the photosynthetic reaction center of Rhodopseudonas viridis, Biochemistry 37 (1998) 2488-2495. (Pubitemid 28119324)
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2488-2495
    • Rabenstein, B.1    Ullmann, G.M.2    Knapp, E.-W.3
  • 171
    • 3042687860 scopus 로고    scopus 로고
    • B redox state in reaction centers from Rhodobacter sphaeroides
    • DOI 10.1021/ja038092q
    • H. Ishikita, E.W. Knapp, Variation of Ser-L223 hydrogen bonding with the QB redox state in reaction centers from Rhodobacter sphaeroides, J. Am. Chem. Soc. 126 (2004) 8059-8064. (Pubitemid 38812797)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.25 , pp. 8059-8064
    • Ishikita, H.1    Knapp, E.-W.2
  • 172
    • 0024650666 scopus 로고
    • In photosynthetic reaction centers, the free energy difference for electron transfer between quinones bound at the primary and secondary quinone-binding sites governs the observed secondary site specificity
    • K.M. Giangiacomo, P.L. Dutton, In photosynthetic reaction centers, the free energy difference for electron transfer between quinones bound at the primary and secondary quinone-binding sites governs the observed secondary site specificity, Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 2658-2662.
    • (1989) Proc. Natl. Acad. Sci. U. S. A , vol.86 , pp. 2658-2662
    • Giangiacomo, K.M.1    Dutton, P.L.2
  • 173
    • 0001354039 scopus 로고
    • Direct charge recombination from D+QAQB - To DQAQB in bacterial reaction centers from Rhodobacter sphaeroides containing low potential quinone in the QA site
    • A. Labahn, J.M. Bruce, M.Y. Okamura, G. Feher, Direct charge recombination from D+QAQB - to DQAQB in bacterial reaction centers from Rhodobacter sphaeroides containing low potential quinone in the QA site, Chem. Phys. 97 (1995) 355-366.
    • (1995) Chem. Phys , vol.97 , pp. 355-366
    • Labahn, A.1    Bruce, J.M.2    Okamura, M.Y.3    Feher, G.4
  • 174
    • 50949087723 scopus 로고    scopus 로고
    • The 2-methoxy group of ubiquinone is essential for function of the acceptor quinones in reaction centers from Rba sphaeroides
    • C.A. Wraight, A.S. Vakkasoglu, Y. Poluektov, A.J. Mattis, D. Nihan, B.H. Lipshutz, The 2-methoxy group of ubiquinone is essential for function of the acceptor quinones in reaction centers from Rba. sphaeroides, Biochim. Biophys. Acta 1777 (2008) 631-636.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 631-636
    • Wraight, C.A.1    Vakkasoglu, A.S.2    Poluektov, Y.3    Mattis, A.J.4    Nihan, D.5    Lipshutz, B.H.6
  • 175
    • 84898770627 scopus 로고    scopus 로고
    • Affinity and activity of non-native quinones at the QB site of bacterial photosynthetic reaction centers
    • (in press)
    • X. Zhang, M.R. Gunner, Affinity and activity of non-native quinones at the QB site of bacterial photosynthetic reaction centers, Photosynth. Res. (2013) (in press).
    • (2013) Photosynth. Res
    • Zhang, X.1    Gunner, M.R.2
  • 176
    • 0035852970 scopus 로고    scopus 로고
    • Trapping conformational intermediate states in the reaction center protein from photosynthetic bacteria
    • DOI 10.1021/bi002326q
    • Q. Xu, M.R. Gunner, Trapping conformational intermediate states in the reaction center protein from photosynthetic bacteria, Biochemistry 40 (2001) 3232-3241. (Pubitemid 32205368)
    • (2001) Biochemistry , vol.40 , Issue.10 , pp. 3232-3241
    • Xu, Q.1    Gunner, M.R.2
  • 177
    • 0037176849 scopus 로고    scopus 로고
    • B electron transfer reaction in bacterial photosynthetic reaction centers: PH dependence of the conformational gating step
    • DOI 10.1021/bi011834c
    • Q. Xu, M.R. Gunner, Exploring the energy profile of the QA - to QB electron transfer reaction in bacterial photosynthetic reaction centers: pH dependence of the conformational gating step, Biochemistry 41 (2002) 2694-2701. (Pubitemid 34168938)
    • (2002) Biochemistry , vol.41 , Issue.8 , pp. 2694-2701
    • Xu, Q.1    Gunner, M.R.2
  • 178
    • 0028967120 scopus 로고
    • Protonation of Glu L212 following QB-formation in the photosynthetic reaction center of Rhodobacter sphaeroides: Evidence from time-resolved infrared spectroscopy
    • R. Hienerwadel, S. Grzybek, C. Fogel, W. Kreutz, M.Y. Okamura, M.L. Paddock, J. Breton, Protonation of Glu L212 following QB-formation in the photosynthetic reaction center of Rhodobacter sphaeroides: evidence from time-resolved infrared spectroscopy, Biochemistry 34 (1995) 2832-2843.
    • (1995) Biochemistry , vol.34 , pp. 2832-2843
    • Hienerwadel, R.1    Grzybek, S.2    Fogel, C.3    Kreutz, W.4    Okamura, M.Y.5    Paddock, M.L.6    Breton, J.7
  • 179
    • 0035923417 scopus 로고    scopus 로고
    • B in reaction centers from Rhodobacter sphaeroides
    • DOI 10.1021/bi011423w
    • E. Nabedryk, J. Breton, M.Y. Okamura, M.L. Paddock, Simultaneous replacement of Asp-L210 and Asp-M17 with Asn increases proton uptake by Glu-L212 upon first electron transfer to QB in reaction centers from Rhodobacter sphaeroides, Biochemistry 40 (2001) 13826-13832. (Pubitemid 33078850)
    • (2001) Biochemistry , vol.40 , Issue.46 , pp. 13826-13832
    • Nabedryk, E.1    Breton, J.2    Okamura, M.Y.3    Paddock, M.L.4
  • 181
    • 30144441164 scopus 로고    scopus 로고
    • Understanding the cytochrome bc complexes by what they don't do. The Q-cycle at 30
    • DOI 10.1016/j.tplants.2005.11.007, PII S1360138505002955
    • J.L. Cape, M.K. Bowman, D.M. Kramer, Understanding the cytochrome bc complexes by what they don't do. The Q-cycle at 30, Trends Plant Sci. 11 (2006) 46-55. (Pubitemid 43053978)
    • (2006) Trends in Plant Science , vol.11 , Issue.1 , pp. 46-55
    • Cape, J.L.1    Bowman, M.K.2    Kramer, D.M.3
  • 182
    • 78149465155 scopus 로고    scopus 로고
    • Activated Q-cycle as a common mechanism for cytochrome bc1 and cytochrome b6f complexes
    • A.Y. Mulkidjanian, Activated Q-cycle as a common mechanism for cytochrome bc1 and cytochrome b6f complexes, Biochim. Biophys. Acta 1797 (2010) 1858-1868.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1858-1868
    • Mulkidjanian, A.Y.1
  • 183
    • 79956128428 scopus 로고    scopus 로고
    • The Q cycle of cytochrome bc complexes: A structure perspective
    • W.A. Cramer, S.S. Hasan, E. Yamashita, The Q cycle of cytochrome bc complexes: a structure perspective, Biochim. Biophys. Acta 1807 (2011) 788-802.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 788-802
    • Cramer, W.A.1    Hasan, S.S.2    Yamashita, E.3
  • 184
    • 57849160616 scopus 로고    scopus 로고
    • Comparison of bacterial reaction centers and photosystem II
    • DOI 10.1007/s11120-008-9369-z
    • L. Kalman, J.C. Williams, J.P. Allen, Comparison of bacterial reaction centers and photosystem II, Photosynth. Res. 98 (2008) 643-655. (Pubitemid 50300661)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 643-655
    • Kalman, L.1    Williams, J.C.2    Allen, J.P.3
  • 185
    • 0030035645 scopus 로고    scopus 로고
    • The conformation of the isoprenyl chain relative to the semiquinone head in the primary electron acceptor (Q(A)) of higher plant PSII (plastosemiquinone) differs from that in bacterial reaction centers (ubisemiquinone or menasemiquinone) by ca. 90
    • DOI 10.1021/bi9522209
    • M. Zheng, C. Dismukes, The conformation of the isoprenyl chain relative to the semiquinone head in the primary electron acceptor (QA) of the higher plant PSII (plastosemiquinone) differs from that in bacterial reaction centers (ubisemiquinone or menasemiquinone) by ca. 90, Biochemistry 35 (1996) 8955-8963. (Pubitemid 26243737)
    • (1996) Biochemistry , vol.35 , Issue.27 , pp. 8955-8963
    • Zheng, M.1    Charles Dismukes, G.2
  • 186
    • 3042812428 scopus 로고    scopus 로고
    • Redox functions of carotenoids in photosynthesis
    • DOI 10.1021/bi0492096
    • H.A. Frank, G.W. Brudvig, Redox functions of carotenoids in photosynthesis, Biochemistry 43 (2004) 8607-8615. (Pubitemid 38880030)
    • (2004) Biochemistry , vol.43 , Issue.27 , pp. 8607-8615
    • Frank, H.A.1    Brudvig, G.W.2
  • 187
    • 79957977505 scopus 로고    scopus 로고
    • Enzymatic function of cytochromeb559 in photosystemII
    • P. Pospisil, Enzymatic function of cytochromeb559 in photosystemII, J. Photochem. Photobiol. B 104 (2011) 341-347.
    • (2011) J. Photochem. Photobiol. B , vol.104 , pp. 341-347
    • Pospisil, P.1
  • 188
    • 12844285876 scopus 로고    scopus 로고
    • Redox potentials of chlorophylls and β-carotene in the antenna complexes of photosystem II
    • DOI 10.1021/ja045058i
    • H. Ishikita, E.-W. Knapp, Redox potentials of chlorophylls and b-carotene in the antenna complexes of photosystem II, J. Am. Chem. Soc. 127 (2005) 1963-1968. (Pubitemid 40229178)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.6 , pp. 1963-1968
    • Ishikita, H.1    Knapp, E.-W.2
  • 189
    • 0026672120 scopus 로고
    • Comparison of structure of quinone redox site in the mitochondrial cytochrome-bc1 complex and photosystem II (QB site)
    • I. Saitoh, H. Miyoshi, R. Shimizu, H. Iwamura, Comparison of structure of quinone redox site in the mitochondrial cytochrome-bc1 complex and photosystem II (QB site), Eur. J. Biochem. 209 (1992) 73-79.
    • (1992) Eur. J. Biochem , vol.209 , pp. 73-79
    • Saitoh, I.1    Miyoshi, H.2    Shimizu, R.3    Iwamura, H.4
  • 190
    • 0002799732 scopus 로고    scopus 로고
    • PhotosystemII and the quinone-iron containing reaction centers: Comparisons and evolutionary perspectives
    • In: H. Baltscheffsky (Ed.) VCH, New York
    • A.W. Rutherford, W. Nitschke, PhotosystemII and the quinone-iron containing reaction centers: comparisons and evolutionary perspectives, in: H. Baltscheffsky (Ed.), Origin and Evolution of Biological Energy Conversion, VCH, New York, 1996, pp. 143-175.
    • (1996) Origin and Evolution of Biological Energy Conversion , pp. 143-175
    • Rutherford, A.W.1    Nitschke, W.2
  • 191
    • 0037007996 scopus 로고    scopus 로고
    • Kinetics and pathways of charge recombination in photosystem II
    • DOI 10.1021/bi025725p
    • F. Rappaport, M. Guergova-Kuras, P.J. Nixon, B.A. Diner, J. Lavergne, Kinetics and pathways of charge recombination in photosystem II, Biochemistry 41 (2002) 8518-8527. (Pubitemid 34705507)
    • (2002) Biochemistry , vol.41 , Issue.26 , pp. 8518-8527
    • Rappaport, F.1    Guergova-Kuras, M.2    Nixon, P.J.3    Diner, B.A.4    Lavergne, J.5
  • 193
    • 0036999722 scopus 로고    scopus 로고
    • Structure, dynamics, and energetics of the primary photochemistry of Photosystem II of oxygenic photosynthesis
    • DOI 10.1146/annurev.arplant.53.100301.135238
    • B.A. Diner, F. Rappaport, Structure, dynamics, and energetics of the primary photochemistry of photosystem II of oxygenic photosynthesis, Annu. Rev. Plant Biol. 53 (2002) 551-580. (Pubitemid 36257507)
    • (2002) Annual Review of Plant Biology , vol.53 , pp. 551-580
    • Diner, B.A.1    Rappaport, F.2
  • 194
    • 33751385171 scopus 로고
    • Structure, spectroscopic, and redox properties of Rhodobacter sphaeroides reaction centers bearing point mutations near the primary electron donor
    • DOI 10.1021/bi00210a041
    • J. Wachtveitl, J.W. Farchaus, R. Das, M. Lutz, B. Robert, T.A. Mattioli, Structure, spectroscopic, and redox properties of Rhodobacter sphaeroides reaction centers bearing point mutations near the primary electron donor, Biochemistry 32 (1993) 12875-12886. (Pubitemid 24005889)
    • (1993) Biochemistry , vol.32 , Issue.47 , pp. 12875-12886
    • Wachtveitl, J.1    Farchaus, J.W.2    Das, R.3    Lutz, M.4    Robert, B.5    Mattioli, T.A.6
  • 195
    • 38049011376 scopus 로고    scopus 로고
    • Primary photochemistry and energetics leading to the oxidation of the Mn4Ca cluster and to the evolution of molecular oxygen in photosystem II
    • F. Rappaport, B.A. Diner, Primary photochemistry and energetics leading to the oxidation of the Mn4Ca cluster and to the evolution of molecular oxygen in photosystem II, Coord. Chem. Rev. 252 (2008) 259-272.
    • (2008) Coord. Chem. Rev , vol.252 , pp. 259-272
    • Rappaport, F.1    Diner, B.A.2
  • 196
    • 0000055138 scopus 로고
    • Function of the two cytochrome components in chloroplasts: A working hypothesis
    • R. Hill, F. Bendall, Function of the two cytochrome components in chloroplasts: a working hypothesis, Nature 186 (1960) 136-137.
    • (1960) Nature , vol.186 , pp. 136-137
    • Hill, R.1    Bendall, F.2
  • 197
    • 0029991064 scopus 로고    scopus 로고
    • Photosynthesis: The Z-scheme revised
    • DOI 10.1016/0968-0004(96)30011-X
    • R.C. Prince, Photosynthesis: the Z-scheme revised, Trends Biochem. Sci. 21 (1996) 121-122. (Pubitemid 26104400)
    • (1996) Trends in Biochemical Sciences , vol.21 , Issue.4 , pp. 121-122
    • Prince, R.C.1
  • 198
    • 0036550933 scopus 로고    scopus 로고
    • The Z-scheme-down hill all the way
    • D.A. Walker, The Z-scheme-down hill all the way, Trends Plant Sci. 7 (2002) 183-185.
    • (2002) Trends Plant Sci , vol.7 , pp. 183-185
    • Walker, D.A.1
  • 200
    • 34147134944 scopus 로고    scopus 로고
    • 4Ca cluster in plant photosystem II membranes studied by polarized range-extended x-ray absorption spectroscopy
    • DOI 10.1074/jbc.M610505200
    • Y. Pushkar, J. Yano, P. Glatzel, J. Messinger, A. Lewis, K. Sauer, U. Bergmann, V. Yachandra, Structure and orientation of the Mn4Ca cluster in plant photosystem II membranes studied by polarized range-extended X-ray absorption spectroscopy, J. Biol. Chem. 282 (2007) 7198-7208. (Pubitemid 47093654)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.10 , pp. 7198-7208
    • Pushkar, Y.1    Yano, J.2    Glatzel, P.3    Messinger, J.4    Lewis, A.5    Sauer, K.6    Bergmann, U.7    Yachandra, V.8
  • 201
    • 38949153095 scopus 로고    scopus 로고
    • 2+ cluster of photosystem II and its protein environment as revealed by X-ray crystallography
    • DOI 10.1098/rstb.2007.2208, PII Q481736325574G47
    • J. Barber, J.W. Murray, The structure of the Mn4Ca2+ cluster of photosystem II and its protein environment as revealed by X-ray crystallography, Phil. Trans. R. Soc. B 363 (2008) 1129-1137. (Pubitemid 351225989)
    • (2008) Philosophical Transactions of the Royal Society B: Biological Sciences , vol.363 , Issue.1494 , pp. 1129-1137
    • Barber, J.1    Murray, J.W.2
  • 202
    • 0032508393 scopus 로고    scopus 로고
    • Role of D1-His190 in proton-coupled electron transfer reactions in photosystem II: A chemical complementation study
    • DOI 10.1021/bi980510u
    • A.M. Hays, I.R. Vassiliev, J.H. Golbeck, R.J. Debus, Role of D1-His190 in proton-coupled electron transfer reactions in photosystem II: a chemical complementation study, Biochemistry 37 (1998) 11352-11365. (Pubitemid 28394885)
    • (1998) Biochemistry , vol.37 , Issue.32 , pp. 11352-11365
    • Hays, A.-M.A.1    Vassiliev, I.R.2    Golbeck, J.H.3    Debus, R.J.4
  • 203
    • 79953057047 scopus 로고    scopus 로고
    • Proton-coupled electron-transfer processes in photosystem II probed by highly resolved g-anisotropy of redox-active tyrosine YZ
    • H. Matsuoka, J.R. Shen, A. Kawamori, K. Nishiyama, Y. Ohba, S. Yamauchi, Proton-coupled electron-transfer processes in photosystem II probed by highly resolved g-anisotropy of redox-active tyrosine YZ, J. Am. Chem. Soc. 133 (2011) 4655-4660.
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 4655-4660
    • Matsuoka, H.1    Shen, J.R.2    Kawamori, A.3    Nishiyama, K.4    Ohba, Y.5    Yamauchi, S.6
  • 204
    • 54949089227 scopus 로고    scopus 로고
    • Geology. The story of O2
    • P.G. Falkowski, Y. Isozaki, Geology. The story of O2, Science 322 (2008) 540-542.
    • (2008) Science , vol.322 , pp. 540-542
    • Falkowski, P.G.1    Isozaki, Y.2
  • 206
    • 79551529447 scopus 로고    scopus 로고
    • The evolutionary pathway from anoxygenic to oxygenic photosynthesis examined by comparison of the properties of photosystem II and bacterial reaction centers
    • J.P. Allen, J.C. Williams, The evolutionary pathway from anoxygenic to oxygenic photosynthesis examined by comparison of the properties of photosystem II and bacterial reaction centers, Photosynth. Res. 107 (2011) 59-69.
    • (2011) Photosynth. Res , vol.107 , pp. 59-69
    • Allen, J.P.1    Williams, J.C.2
  • 207
    • 0014805072 scopus 로고
    • Cooperation of charges in photosynthetic O2 evolution-I. A linear four step mechanism
    • B. Kok, B. Forbush, M. McGloin, Cooperation of charges in photosynthetic O2 evolution-I. A linear four step mechanism, Photochem. Photobiol. 11 (1970) 457-475.
    • (1970) Photochem. Photobiol , vol.11 , pp. 457-475
    • Kok, B.1    Forbush, B.2    McGloin, M.3
  • 208
    • 13644271567 scopus 로고    scopus 로고
    • 0) characterized by X-ray absorption spectroscopy at 20 K and room temperature
    • DOI 10.1021/bi048697e
    • M. Haumann, C. Mueller, P. Liebisch, L. Iuzzolino, J. Dittmer, M. Grabolle, T. Neisius, W. Meyer-Klaucke, H. Dau, Structural and oxidation state changes of the photosystem II manganese complex in four transitions of the water oxidation cycle (S0 → S1, S1 → S2, S2 → S3, and S3,4 → S0) characterized by X-ray absorption spectroscopy at 20 K and room temperature, Biochemistry 44 (2005) 1894-1908. (Pubitemid 40227473)
    • (2005) Biochemistry , vol.44 , Issue.6 , pp. 1894-1908
    • Haumann, M.1    Muller, C.2    Liebisch, P.3    Iuzzolino, L.4    Dittmer, J.5    Grabolle, M.6    Neisius, T.7    Meyer-Klaucke, W.8    Dau, H.9
  • 209
    • 77954196565 scopus 로고    scopus 로고
    • Energy conversion in natural and artificial photosynthesis
    • I. McConnell, G. Li, G.W. Brudvig, Energy conversion in natural and artificial photosynthesis, Chem. Biol. 17 (2010) 434-447.
    • (2010) Chem. Biol , vol.17 , pp. 434-447
    • McConnell, I.1    Li, G.2    Brudvig, G.W.3
  • 210
    • 0032497927 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy on layered photosystem IImembrane particles suggests manganesecentered oxidation of the oxygen-evolving complex for the S0-S1
    • L. Iuzzolino, J. Dittmer, W. Doerner, W. Meyer-Klaucke, H. Dau, X-ray absorption spectroscopy on layered photosystem IImembrane particles suggests manganesecentered oxidation of the oxygen-evolving complex for the S0-S1, S1-S2, and S2-S3 transitions of the water oxidation cycle, Biochemistry 37 (1998) 17112-17119.
    • (1998) S1-S2, and S2-S3 Transitions of the Water Oxidation Cycle, Biochemistry , vol.37 , pp. 17112-17119
    • Iuzzolino, L.1    Dittmer, J.2    Doerner, W.3    Meyer-Klaucke, W.4    Dau, H.5
  • 211
    • 0023426051 scopus 로고
    • Tyrosine radicals are involved in the photosynthetic oxygen-evolving system
    • B.A. Barry, G.T. Babcock, Tyrosine radicals are involved in the photosynthetic oxygen-evolving system, Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 7099-7103.
    • (1987) Proc. Natl. Acad. Sci. U. S. A , vol.84 , pp. 7099-7103
    • Barry, B.A.1    Babcock, G.T.2
  • 212
    • 0034640197 scopus 로고    scopus 로고
    • Proton and hydrogen currents in photosynthetic water oxidation
    • DOI 10.1016/S0005-2728(00)00069-4, PII S0005272800000694
    • C. Tommos, G.T. Babcock, Proton and hydrogen currents in photosynthetic water oxidation, Biochim. Biophys. Acta 1458 (2000) 199-219. (Pubitemid 30254260)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1458 , Issue.1 , pp. 199-219
    • Tommos, C.1    Babcock, G.T.2
  • 214
    • 84863116216 scopus 로고    scopus 로고
    • Proton coupled electron transfer and redox active tyrosines: Structure and function of the tyrosyl radicals in ribonucleotide reductase and photosystem II
    • B.A. Barry, J. Chen, J. Keough, D. Jenson, A. Offenbacher, C. Pagba, Proton coupled electron transfer and redox active tyrosines: structure and function of the tyrosyl radicals in ribonucleotide reductase and photosystem II, J. Phys. Chem. Lett. 3 (2012) 543-554.
    • (2012) J. Phys. Chem. Lett , vol.3 , pp. 543-554
    • Barry, B.A.1    Chen, J.2    Keough, J.3    Jenson, D.4    Offenbacher, A.5    Pagba, C.6
  • 215
    • 33748716572 scopus 로고
    • Determination of the acidity constants of some phenol radical cations by means of electron spin resonance
    • W.T. Dixon, D. Murphy, Determination of the acidity constants of some phenol radical cations by means of electron spin resonance, J. Chem. Soc. Faraday Trans. 72 (1972).
    • (1972) J. Chem. Soc. Faraday Trans , vol.72
    • Dixon, W.T.1    Murphy, D.2
  • 216
  • 217
    • 80455129436 scopus 로고    scopus 로고
    • Electrochemical and structural properties of a protein system designed to generate tyrosine pourbaix diagrams
    • M.C. Martínez-Rivera, B.W. Berry, K.G. Valentine, K. Westerlund, S. Hay, C. Tommos, Electrochemical and structural properties of a protein system designed to generate tyrosine pourbaix diagrams, J. Am. Chem. Soc. 133 (2011) 17786-17795.
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 17786-17795
    • Martínez-Rivera, M.C.1    Berry, B.W.2    Valentine, K.G.3    Westerlund, K.4    Hay, S.5    Tommos, C.6
  • 218
    • 0030668554 scopus 로고    scopus 로고
    • The natural selection of the chemical elements
    • DOI 10.1007/s000180050102
    • R.J. Williams, The natural selection of the chemical elements, Cell. Mol. Life Sci. 53 (1997) 816-829. (Pubitemid 27507533)
    • (1997) Cellular and Molecular Life Sciences , vol.53 , Issue.10 , pp. 816-829
    • Williams, R.J.P.1
  • 219
    • 0041707971 scopus 로고    scopus 로고
    • A combined experimental and theoretical study of divalent metal ion selectivity and function in proteins: Application to E. Coli ribonuclease H1
    • DOI 10.1021/ja034956w
    • C.S. Babu, T. Dudev, R. Casareno, J.A. Cowan, C. Lim, A combined experimental and theoretical study of divalent metal ion selectivity and function in proteins: application to E. coli ribonuclease H1, J. Am. Chem. Soc. 125 (2003) 9318-9328. (Pubitemid 36936051)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.31 , pp. 9318-9328
    • Babu, C.S.1    Dudev, T.2    Casareno, R.3    Cowan, J.A.4    Lim, C.5
  • 221
    • 15744392732 scopus 로고    scopus 로고
    • 2+ in metalloproteins: A DFT/CDM study
    • DOI 10.1021/ja044404t
    • T. Dudev, L.Y. Chang, C. Lim, Factors governing the substitution of La3+ for Ca2+ and Mg2+ in metalloproteins: a DFT/CDM study, J. Am. Chem. Soc. 127 (2005) 4091-4103. (Pubitemid 40411451)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.11 , pp. 4091-4103
    • Dudev, T.1    Chang, L.-Y.2    Lim, C.3
  • 222
    • 48249153490 scopus 로고    scopus 로고
    • Metal binding affinity and selectivity in metalloproteins: Insights from computational studies
    • T. Dudev, C. Lim, Metal binding affinity and selectivity in metalloproteins: insights from computational studies, Annu. Rev. Biophys. 37 (2008) 97-116.
    • (2008) Annu. Rev. Biophys , vol.37 , pp. 97-116
    • Dudev, T.1    Lim, C.2
  • 223
    • 70349241668 scopus 로고    scopus 로고
    • Metal-binding affinity and selectivity of nonstandard natural amino acid residues from DFT/CDM calculations
    • T. Dudev, C. Lim, Metal-binding affinity and selectivity of nonstandard natural amino acid residues from DFT/CDM calculations, J. Phys. Chem. B 113 (2009) 11754-11764.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 11754-11764
    • Dudev, T.1    Lim, C.2
  • 226
    • 84862188888 scopus 로고    scopus 로고
    • Why nature chose Mn for the water oxidase in photosystem II
    • R.J. Pace, R. Stranger, S. Petrie, Why nature chose Mn for the water oxidase in photosystem II, Dalton Trans. 41 (2012) 7179-7189.
    • (2012) Dalton Trans , vol.41 , pp. 7179-7189
    • Pace, R.J.1    Stranger, R.2    Petrie, S.3
  • 228
    • 43649098548 scopus 로고    scopus 로고
    • Redox tuning over almost 1 v in a structurally conserved active site: Lessons from Fe-containing superoxide dismutase
    • A.F. Miller, Redox tuning over almost 1 V in a structurally conserved active site: lessons from Fe-containing superoxide dismutase, Acc. Chem. Res. 41 (2008) 501-510.
    • (2008) Acc. Chem. Res , vol.41 , pp. 501-510
    • Miller, A.F.1
  • 229
    • 0037248891 scopus 로고    scopus 로고
    • Proton-coupled electron transfer in Fe-superoxide dismutase and Mn-superoxide dismutase
    • DOI 10.1016/S0162-0134(02)00621-9
    • A.F. Miller, K. Padmakumar, D.L. Sorkin, A. Karapetian, C.K. Vance, Proton-coupled electron transfer in Fe-superoxide dismutase and Mn-superoxide dismutase, J. Inorg. Biochem. 93 (2003) 71-83. (Pubitemid 36132136)
    • (2003) Journal of Inorganic Biochemistry , vol.93 , Issue.1-2 , pp. 71-83
    • Miller, A.-F.1    Padmakumar, K.2    Sorkin, D.L.3    Karapetian, A.4    Vance, C.K.5
  • 231
    • 4243989332 scopus 로고
    • Electron paramagnetic resonance properties of the S2 state of the oxygen-evolving complex of photosystem II
    • J.L. Zimmermann, A.W. Rutherford, Electron paramagnetic resonance properties of the S2 state of the oxygen-evolving complex of photosystem II, Biochemistry 25 (1986) 4609-4615.
    • (1986) Biochemistry , vol.25 , pp. 4609-4615
    • Zimmermann, J.L.1    Rutherford, A.W.2
  • 232
    • 33751424725 scopus 로고    scopus 로고
    • Water-splitting chemistry of photosystem II
    • DOI 10.1021/cr0204294
    • J.P. McEvoy, G.W. Brudvig, Water-splitting chemistry of photosystem II, Chem. Rev. 106 (2006) 4455-4483. (Pubitemid 44816649)
    • (2006) Chemical Reviews , vol.106 , Issue.11 , pp. 4455-4483
    • McEvoy, J.P.1    Brudvig, G.W.2
  • 233
    • 42149091731 scopus 로고    scopus 로고
    • Multifrequency pulsed electron paramagnetic resonance study of the S-2 state of the photosystem II manganese cluster
    • G.J. Yeagle, M.L. Gilchrist, R.M. McCarrick, R.D. Britt, Multifrequency pulsed electron paramagnetic resonance study of the S-2 state of the photosystem II manganese cluster, Inorg. Chem. 47 (2008) 1803-1814.
    • (2008) Inorg. Chem , vol.47 , pp. 1803-1814
    • Yeagle, G.J.1    Gilchrist, M.L.2    McCarrick, R.M.3    Britt, R.D.4
  • 234
    • 32544444622 scopus 로고    scopus 로고
    • Factors governing the metal coordination number in metal complexes from cambridge structural database analyses
    • DOI 10.1021/jp054975n
    • M. Dudev, J. Wang, T. Dudev, C. Lim, Factors governing the metal coordination number in metal complexes from Cambridge Structural Database analyses, J. Phys. Chem. B 110 (2006) 1889-1895. (Pubitemid 43235791)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.4 , pp. 1889-1895
    • Dudev, M.1    Wang, J.2    Dudev, T.3    Lim, C.4
  • 235
    • 33747613338 scopus 로고    scopus 로고
    • Competition between protein ligands and cytoplasmic inorganic anions for the metal cation: A DFT/CDM study
    • DOI 10.1021/ja063111s
    • T. Dudev, C. Lim, Competition between protein ligands and cytoplasmic inorganic anions for the metal cation: a DFT/CDM study, J. Am. Chem. Soc. 128 (2006) 10541-10548. (Pubitemid 44265096)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.32 , pp. 10541-10548
    • Dudev, T.1    Lim, C.2
  • 236
    • 32244438113 scopus 로고    scopus 로고
    • A DFT/CDM study of metal-carboxylate interactions in metalloproteins: Factors governing the maximum number of metal-bound carboxylates
    • DOI 10.1021/ja055797e
    • T. Dudev, C. Lim, A DFT/CDM study of metal-carboxylate interactions in metalloproteins: factors governing the maximum number of metal-bound carboxylates, J. Am. Chem. Soc. 128 (2006) 1553-1561. (Pubitemid 43214867)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.5 , pp. 1553-1561
    • Dudevt, T.1    Lim, C.2
  • 238
    • 78650581853 scopus 로고    scopus 로고
    • Proton-coupled electron flow in protein redox machines
    • J.L. Dempsey, J.R. Winkler, H.B. Gray, Proton-coupled electron flow in protein redox machines, Chem. Rev. 110 (2010) 7024-7039.
    • (2010) Chem. Rev , vol.110 , pp. 7024-7039
    • Dempsey, J.L.1    Winkler, J.R.2    Gray, H.B.3
  • 239
    • 36849008128 scopus 로고    scopus 로고
    • Proton-coupled electron transfer
    • DOI 10.1021/cr0500030
    • M.H. Huynh, T.J. Meyer, Proton-coupled electron transfer, Chem. Rev. 107 (2007) 5004-5064. (Pubitemid 350225868)
    • (2007) Chemical Reviews , vol.107 , Issue.11 , pp. 5004-5064
    • Huynh, M.H.V.1    Meyer, T.J.2
  • 240
    • 0001720878 scopus 로고
    • The effect of protonation on Mn(IV)(μ-O)2 complexes
    • M.J. Baldwin, A. Gelasco, V.L. Pecoraro, The effect of protonation on Mn(IV)(μ-O)2 complexes, Photosynth. Res. 38 (1993) 303-308.
    • (1993) Photosynth. Res. , vol.38 , pp. 303-308
    • Baldwin, M.J.1    Gelasco, A.2    Pecoraro, V.L.3
  • 241
    • 0029909232 scopus 로고    scopus 로고
    • Energetics of proton-coupled electron transfer in high-valent Mn2(μ-O)2 systems: Models for water oxidation by the oxygen-evolving complex of photosystem II
    • M.J. Baldwin, V.L. Pecoraro, Energetics of proton-coupled electron transfer in high-valent Mn2(μ-O)2 systems: models for water oxidation by the oxygen-evolving complex of photosystem II, J. Am. Chem. Soc. 118 (1996) 11325.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 11325
    • Baldwin, M.J.1    Pecoraro, V.L.2
  • 242
    • 38049092500 scopus 로고    scopus 로고
    • Functional models for the oxygen-evolving complex of photosystem II
    • C.W. Cady, R.H. Crabtree, G.W. Brudvig, Functional models for the oxygen-evolving complex of photosystem II, Coord. Chem. Rev. 252 (2008) 444-455.
    • (2008) Coord. Chem. Rev , vol.252 , pp. 444-455
    • Cady, C.W.1    Crabtree, R.H.2    Brudvig, G.W.3
  • 244
    • 0030956950 scopus 로고    scopus 로고
    • Thermodynamic viability of hydrogen atom transfer from water coordinated to the oxygen-evolving complex of photosystem II
    • DOI 10.1021/ja9641158, PII S0002786396041157
    • M.T. Caudle, V.L. Pecoraro, Thermodynamic viability of hydrogen atom transfer from water coordinated to the oxygen-evolving complex of photosystem II, J. Am. Chem. Soc. 119 (1997) 3415-3416. (Pubitemid 27213859)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.14 , pp. 3415-3416
    • Caudle, M.T.1    Pecoraro, V.L.2
  • 245
    • 0002124260 scopus 로고
    • Acidity of hydrido transition metal complexes in solution
    • A. Dedieu (Ed.), VCH Publishers
    • S. Kristjánsdóttir, J. Norton, Acidity of hydrido transition metal complexes in solution, in: A. Dedieu (Ed.), Transition Metal Hydrides, VCH Publishers, 1992, pp. 309-359.
    • (1992) Transition Metal Hydrides , pp. 309-359
    • Kristjánsdóttir, S.1    Norton, J.2
  • 246
    • 84878035773 scopus 로고    scopus 로고
    • A simple classical model to study high-valent oxomanganese model complexes and their relevance to the oxygen evolving complex of photosystem II
    • M. Amin, L. Vogt, S. Vassiliev, I. Rivalta, D. Bruce, G.W. Brudvig, V.S. Batista, M.R. Gunner, A simple classical model to study high-valent oxomanganese model complexes and their relevance to the oxygen evolving complex of photosystem II, J. Phys. Chem B. (2013), http://dx.doi.org/10.1021/jp403321b.
    • (2013) J. Phys. Chem B
    • Amin, M.1    Vogt, L.2    Vassiliev, S.3    Rivalta, I.4    Bruce, D.5    Brudvig, G.W.6    Batista, V.S.7    Gunner, M.R.8
  • 247
    • 84860791053 scopus 로고    scopus 로고
    • Oxygen-evolving Mn cluster in photosystem II: The protonation pattern and oxidation state in the high-resolution crystal structure
    • A. Galstyan, A. Robertazzi, E.W. Knapp, Oxygen-evolving Mn cluster in photosystem II: the protonation pattern and oxidation state in the high-resolution crystal structure, J. Am. Chem. Soc. 134 (2012) 7442-7449.
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 7442-7449
    • Galstyan, A.1    Robertazzi, A.2    Knapp, E.W.3
  • 249
    • 29244488966 scopus 로고    scopus 로고
    • Computational structural model of the oxygen evolving complex in photosystem II: Complete ligation by protein, water and chloride
    • D. Bruce, A. van der Est (Eds.) Allen Press, Lawrence, Kansas
    • J.P. McEvoy, J.A. Gascon, E.M. Sproviero, V.S. Batista, G.W. Brudvig, Computational structural model of the oxygen evolving complex in photosystem II: complete ligation by protein, water and chloride, in: D. Bruce, A. van der Est (Eds.), Photosynthesis: Fundamental Aspects to Global Perspectives, Allen Press, Lawrence, Kansas, 2005, pp. 278-280.
    • (2005) Photosynthesis: Fundamental Aspects to Global Perspectives , pp. 278-280
    • McEvoy, J.P.1    Gascon, J.A.2    Sproviero, E.M.3    Batista, V.S.4    Brudvig, G.W.5
  • 251
    • 34147161261 scopus 로고    scopus 로고
    • Quantum mechanics/molecular mechanics structural models of the oxygen-evolving complex of photosystem II
    • DOI 10.1016/j.sbi.2007.03.015, PII S0959440X07000450, Theory and Simulation / Mecromolecular Assemblages
    • E.M. Sproviero, J.A. Gascon, J.P. McEvoy, G.W. Brudvig, V.S. Batista, Quantum mechanics/molecular mechanics structural models of the oxygenevolving complex of photosystem II, Curr. Opin. Struct. Biol. 17 (2007) 173-180. (Pubitemid 46575260)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.2 , pp. 173-180
    • Sproviero, E.M.1    Gascon, J.A.2    McEvoy, J.P.3    Brudvig, G.W.4    Batista, V.S.5
  • 254
    • 84862511715 scopus 로고    scopus 로고
    • A comparison of two-electron chemistry performed by the manganese and iron heterodimer and homodimers
    • K. Roos, P.E. Siegbahn, A comparison of two-electron chemistry performed by the manganese and iron heterodimer and homodimers, J. Biol. Inorg. Chem. 17 (2012) 363-373.
    • (2012) J. Biol. Inorg. Chem , vol.17 , pp. 363-373
    • Roos, K.1    Siegbahn, P.E.2
  • 255
    • 84860754998 scopus 로고    scopus 로고
    • How is methane formed and oxidized reversibly when catalyzed by Ni-containing methyl-coenzyme M reductase?
    • S.L. Chen, M.R. Blomberg, P.E. Siegbahn, How is methane formed and oxidized reversibly when catalyzed by Ni-containing methyl-coenzyme M reductase? Chemistry 18 (2012) 6309-6315.
    • (2012) Chemistry , vol.18 , pp. 6309-6315
    • Chen, S.L.1    Blomberg, M.R.2    Siegbahn, P.E.3
  • 257
    • 72749109576 scopus 로고    scopus 로고
    • Water oxidation in photosystem II: Oxygen release, proton release and the effect of chloride
    • P.E.M. Siegbahn, Water oxidation in photosystem II: oxygen release, proton release and the effect of chloride, Dalton Trans. (2009) 10063-10068.
    • (2009) Dalton Trans , pp. 10063-10068
    • Siegbahn, P.E.M.1
  • 258
    • 84867548419 scopus 로고    scopus 로고
    • Modeling near-edge fine structure X-ray spectra of the manganese catalytic site for water oxidation in photosystem II
    • B. Brena, P.E. Siegbahn, H. Agren, Modeling near-edge fine structure X-ray spectra of the manganese catalytic site for water oxidation in photosystem II, J. Am. Chem. Soc. 134 (2012) 17157-17167.
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 17157-17167
    • Brena, B.1    Siegbahn, P.E.2    Agren, H.3
  • 259
    • 29244479217 scopus 로고    scopus 로고
    • The mechanism for dioxygen formation in PSII studied by quantum chemical methods
    • DOI 10.1039/b506746b
    • P.E.M. Siegbahn, M. Lundberg, The mechanism for dioxygen formation in PSII studied by quantum chemical methods, Photochem. Photobiol. Sci. 4 (2005) 1035-1043. (Pubitemid 41818864)
    • (2005) Photochemical and Photobiological Sciences , vol.4 , Issue.12 , pp. 1035-1043
    • Siegbahn, P.E.M.1    Lundberg, M.2
  • 260
    • 33646138247 scopus 로고    scopus 로고
    • Hydroxide instead of bicarbonate in the structure of the oxygen evolving complex
    • P.E.M. Siegbahn, M. Lundberg, Hydroxide instead of bicarbonate in the structure of the oxygen evolving complex, J. Inorg. Biochem. 100 (2006) 1035-1040.
    • (2006) J. Inorg. Biochem , vol.100 , pp. 1035-1040
    • Siegbahn, P.E.M.1    Lundberg, M.2
  • 262
    • 83055161471 scopus 로고    scopus 로고
    • Theoretical evaluation of structural models of the S2 state in the oxygen evolving complex of photosystem II: Protonation states and magnetic interactions
    • W. Ames, D.A. Pantazis, V. Krewald, N. Cox, J. Messinger, W. Lubitz, F. Neese, Theoretical evaluation of structural models of the S2 state in the oxygen evolving complex of photosystem II: protonation states and magnetic interactions, J. Am. Chem. Soc. 133 (2011) 19743-19757.
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 19743-19757
    • Ames, W.1    Pantazis, D.A.2    Krewald, V.3    Cox, N.4    Messinger, J.5    Lubitz, W.6    Neese, F.7
  • 263
    • 84879514598 scopus 로고    scopus 로고
    • Water oxidation mechanism in photosystem II, including oxidations, proton release pathways, O\O bond formation and O2 release
    • (Electronic publication ahead of print)
    • P.E. Siegbahn, Water oxidation mechanism in photosystem II, including oxidations, proton release pathways, O\O bond formation and O2 release, Biochim. Biophys. Acta (2012) (Electronic publication ahead of print).
    • (2012) Biochim. Biophys. Acta
    • Siegbahn, P.E.1
  • 264
    • 77955875343 scopus 로고    scopus 로고
    • Ligand environment of the S2 state of photosystem II: A study of the hyperfine interactions of the tetranuclear manganese cluster by 2D 14 N HYSCORE spectroscopy
    • S. Milikisiyants, R. Chatterjee, A. Weyers, A. Meenaghan, C. Coates, K.V. Lakshmi, Ligand environment of the S2 state of photosystem II: a study of the hyperfine interactions of the tetranuclear manganese cluster by 2D 14 N HYSCORE spectroscopy, J. Phys. Chem. B 114 (2010) 10905-10911.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 10905-10911
    • Milikisiyants, S.1    Chatterjee, R.2    Weyers, A.3    Meenaghan, A.4    Coates, C.5    Lakshmi, K.V.6
  • 265
    • 67650517036 scopus 로고    scopus 로고
    • Monitoring proton release during photosynthetic water oxidation in photosystem II by means of isotope-edited infrared spectroscopy
    • H. Suzuki, M. Sugiura, T. Noguchi, Monitoring proton release during photosynthetic water oxidation in photosystem II by means of isotope-edited infrared spectroscopy, J. Am. Chem. Soc. 131 (2009) 7849-7857.
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 7849-7857
    • Suzuki, H.1    Sugiura, M.2    Noguchi, T.3
  • 266
    • 0026665269 scopus 로고
    • Proton release during the four steps of photosynthetic water oxidation: Induction of 1:1:1:1 pattern due to lack of chlorophyll a/b binding proteins
    • P. Jahns, W. Junge, Proton release during the four steps of photosynthetic water oxidation: induction of 1:1:1:1 pattern due to lack of chlorophyll a/b binding proteins, Biochemistry 31 (1992) 7398-7403.
    • (1992) Biochemistry , vol.31 , pp. 7398-7403
    • Jahns, P.1    Junge, W.2
  • 269
    • 79957621833 scopus 로고    scopus 로고
    • Role of Arg82 in the early steps of the bacteriorhodopsin proton-pumping cycle
    • M. Clemens, P. Phatak, Q. Cui, A.N. Bondar, M. Elstner, Role of Arg82 in the early steps of the bacteriorhodopsin proton-pumping cycle, J. Phys. Chem. B 115 (2011) 7129-7135.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 7129-7135
    • Clemens, M.1    Phatak, P.2    Cui, Q.3    Bondar, A.N.4    Elstner, M.5
  • 270
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 Ångstrom resolution
    • H. Luecke, B. Schobert, H.T. Richter, J.P. Cartailler, J.K. Lanyi, Structural changes in bacteriorhodopsin during ion transport at 2 Ångstrom resolution, Science 286 (1999) 255-261.
    • (1999) Science , vol.286 , pp. 255-261
    • Luecke, H.1    Schobert, B.2    Richter, H.T.3    Cartailler, J.P.4    Lanyi, J.K.5
  • 274
    • 0030770570 scopus 로고    scopus 로고
    • 2 transition
    • B. Hessling, J. Herbst, R. Rammelsberg, K. Gerwert, Fourier transform infrared double-flash experiments resolve bacteriorhodopsin's M1 to M2 transition, Biophys. J. 73 (1997) 2071-2080. (Pubitemid 27425737)
    • (1997) Biophysical Journal , vol.73 , Issue.4 , pp. 2071-2080
    • Hessling, B.1    Herbst, J.2    Rammelsberg, R.3    Gerwert, K.4
  • 275
    • 0032492706 scopus 로고    scopus 로고
    • Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network
    • DOI 10.1021/bi971701k
    • R. Rammelsberg, G. Huhn, M. Lubben, K. Gerwert, Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network, Biochemistry 37 (1998) 5001-5009. (Pubitemid 28175982)
    • (1998) Biochemistry , vol.37 , Issue.14 , pp. 5001-5009
    • Rammelsberg, R.1    Huhn, G.2    Lubben, M.3    Gerwert, K.4
  • 276
    • 0035016932 scopus 로고    scopus 로고
    • Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin
    • N. Radzwill, K. Gerwert, H.J. Steinhoff, Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin, Biophys. J. 80 (2001) 2856-2866. (Pubitemid 32521658)
    • (2001) Biophysical Journal , vol.80 , Issue.6 , pp. 2856-2866
    • Radzwill, N.1    Gerwert, K.2    Steinhoff, H.-J.3
  • 277
    • 79960979207 scopus 로고    scopus 로고
    • Proton transfer via a transient linear water-molecule chain in a membrane protein
    • E. Freier, S. Wolf, K. Gerwert, Proton transfer via a transient linear water-molecule chain in a membrane protein, Proc. Natl. Acad. Sci. U. S. A. 108 (2011) 11435-11439.
    • (2011) Proc. Natl. Acad. Sci. U. S. A , vol.108 , pp. 11435-11439
    • Freier, E.1    Wolf, S.2    Gerwert, K.3
  • 279
    • 0038053899 scopus 로고    scopus 로고
    • Structural insights into the mechanism of proton pumping by bacteriorhodopsin
    • DOI 10.1016/S0014-5793(03)00386-7
    • T. Hirai, S. Subramaniam, Structural insights into the mechanism of proton pumping by bacteriorhodopsin, FEBS Lett. 545 (2003) 2-8. (Pubitemid 36629629)
    • (2003) FEBS Letters , vol.545 , Issue.1 , pp. 2-8
    • Hirai, T.1    Subramaniam, S.2
  • 280
    • 0028023207 scopus 로고
    • PH-induced structural changes in bacteriorhodopsin studied by Fourier transform infrared spectroscopy
    • S. Szaraz, D. Oesterhelt, P. Ormos, pH-induced structural-changes in bacteriorhodopsin studied by Fourier-transform infrared-spectroscopy, Biophys. J. 67 (1994) 1706-1712. (Pubitemid 24304342)
    • (1994) Biophysical Journal , vol.67 , Issue.4 , pp. 1706-1712
    • Szaraz, S.1    Oesterhelt, D.2    Ormos, P.3
  • 281
    • 0035345448 scopus 로고    scopus 로고
    • Trapping and spectroscopic identification of the photointermediates of bacteriorhodopsin at low temperatures
    • S.P. Balashov, T.G. Ebrey, Trapping and spectroscopic identification of the photointermediates of bacteriorhodopsin at low temperatures, Photochem. Photobiol. 73 (2001) 453-462. (Pubitemid 33720355)
    • (2001) Photochemistry and Photobiology , vol.73 , Issue.5 , pp. 453-462
    • Balashov, S.P.1    Ebrey, T.G.2
  • 282
    • 50949124924 scopus 로고    scopus 로고
    • Xanthorhodopsin: A bacteriorhodopsin-like proton pump with a carotenoid antenna
    • J.K. Lanyi, S.P. Balashov, Xanthorhodopsin: a bacteriorhodopsin-like proton pump with a carotenoid antenna, Biochim. Biophys. Acta 1777 (2008) 684-688.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 684-688
    • Lanyi, J.K.1    Balashov, S.P.2
  • 284
    • 0035823064 scopus 로고    scopus 로고
    • a calculations suggest storage of an excess proton in a hydrogen-bonded water network in bacteriorhodopsin
    • DOI 10.1006/jmbi.2001.4902
    • V.Z. Spassov, H. Luecke, K. Gerwert, D. Bashford, pKa calculations suggest storage of an excess proton in a hydrogen-bonded water network in bacteriorhodopsin, J. Mol. Biol. 312 (2001) 203-219. (Pubitemid 32835687)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.1 , pp. 203-219
    • Spassov, V.Z.1    Luecke, H.2    Gerwert, K.3    Bashford, D.4
  • 285
    • 3142613053 scopus 로고    scopus 로고
    • Mechanism of primary proton transfer in bacteriorhodopsin
    • DOI 10.1016/j.str.2004.04.016, PII S0969212604001637
    • A.N. Bondar, M. Elstner, S. Suhai, J.C. Smith, S. Fischer, Mechanism of primary proton transfer in bacteriorhodopsin, Structure 12 (2004) 1281-1288. (Pubitemid 38900770)
    • (2004) Structure , vol.12 , Issue.7 , pp. 1281-1288
    • Bondar, A.-N.1    Elstner, M.2    Suhai, S.3    Smith, J.C.4    Fischer, S.5
  • 287
    • 4944249406 scopus 로고    scopus 로고
    • 15N-labeled arginine
    • DOI 10.1021/bi049238g
    • Y. Xiao, M.S. Hutson, M. Belenky, J. Herzfeld, M.S. Braiman, Role of arginine-82 in fast proton release during the bacteriorhodopsin photocycle: a time-resolved FT-IR study of purple membranes containing 15N-labeled arginine, Biochemistry 43 (2004) 12809-12818. (Pubitemid 39331800)
    • (2004) Biochemistry , vol.43 , Issue.40 , pp. 12809-12818
    • Xiao, Y.1    Hutson, M.S.2    Belenky, M.3    Herzfeld, J.4    Braiman, M.S.5
  • 288
    • 0038649076 scopus 로고    scopus 로고
    • Crystallographic structures of the M and N intermediates of bacteriorhodopsin: Assembly of a hydrogen-bonded chain of water molecules between Asp-96 and the retinal Schiff base
    • DOI 10.1016/S0022-2836(03)00576-X
    • B. Schobert, L.S. Brown, J.K. Lanyi, Crystallographic structures of the M and N intermediates of bacteriorhodopsin: assembly of a hydrogen-bonded chain of water molecules between Asp-96 and the retinal Schiff base, J. Mol. Biol. 330 (2003) 553-570. (Pubitemid 36814053)
    • (2003) Journal of Molecular Biology , vol.330 , Issue.3 , pp. 553-570
    • Schobert, B.1    Brown, L.S.2    Lanyi, J.K.3
  • 289
    • 0029665673 scopus 로고    scopus 로고
    • A linkage of the pK(a)'s of asp-85 and glu-204 forms part of the reprotonation switch of bacteriorhodopsin
    • DOI 10.1021/bi952883q
    • H.T. Richter, L.S. Brown, R. Needleman, J.K. Lanyi, A linkage of the pka's of asp-85 and glu-204 forms part of the reprotonation switch of bateriorhodopsin, Biochemistry 35 (1996) 4054-4062. (Pubitemid 26113461)
    • (1996) Biochemistry , vol.35 , Issue.13 , pp. 4054-4062
    • Richter, H.-T.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 290
    • 2542464946 scopus 로고    scopus 로고
    • Coupled proton and electron transfer reactions in cytochrome oxidase
    • d505-999
    • R.B. Gennis, Coupled proton and electron transfer reactions in cytochrome oxidase, Front. Biosci. 9 (2004) 581-591. (Pubitemid 39043736)
    • (2004) Frontiers in Bioscience , vol.9 , pp. 581-591
    • Gennis, R.B.1
  • 291
    • 84857921525 scopus 로고    scopus 로고
    • The mechanism for proton pumping in cytochrome c oxidase from an electrostatic and quantum chemical perspective
    • M.R. Blomberg, P.E. Siegbahn, The mechanism for proton pumping in cytochrome c oxidase from an electrostatic and quantum chemical perspective, Biochim. Biophys. Acta 1817 (2012) 495-505.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 495-505
    • Blomberg, M.R.1    Siegbahn, P.E.2
  • 292
    • 0017883558 scopus 로고
    • Involvement of intramitochondrial protons in redox reactions of cytochrome a
    • DOI 10.1016/0014-5793(78)80327-5
    • V.Y. Artzatbanov, A.A. Konstantinov, V.P. Skulachev, Involvement of intramitochondrial protons in redox reactions of cytochrome alpha, FEBS Lett. 87 (1978) 180-185. (Pubitemid 8280815)
    • (1978) FEBS Letters , vol.87 , Issue.2 , pp. 180-185
    • Artzatbanov Yu., V.1    Konstantinov, A.A.2    Skulachev, V.P.3
  • 293
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: Implications for mechanism of electron-proton transfer
    • DOI 10.1126/science.276.5313.812
    • M.H.B. Stowell, T.M. McPhillips, D.C. Rees, S.M. Soltis, E. Abresch, G. Feher, Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer, Science 276 (1997) 812-816. (Pubitemid 27199864)
    • (1997) Science , vol.276 , Issue.5313 , pp. 812-816
    • Stowell, M.H.B.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 297
    • 0034711407 scopus 로고    scopus 로고
    • Oxygen activation and reduction in respiration involvement of redox-active tyrosine 244
    • D.A. Proshlyakov, M.A. Pressler, C. Demaso, J.F. Leykam, D.L. Dewitt, G.T. Babcock, Oxygen activation and reduction in respiration involvement of redox-active tyrosine 244, Science 290 (2000) 1588-1591.
    • (2000) Science , vol.290 , pp. 1588-1591
    • Proshlyakov, D.A.1    Pressler, M.A.2    Demaso, C.3    Leykam, J.F.4    Dewitt, D.L.5    Babcock, G.T.6
  • 298
    • 0032311172 scopus 로고    scopus 로고
    • From water to oxygen and back again: Mechanistic similarities in the enzymatic redox conversions between water and dioxygen
    • DOI 10.1016/S0005-2728(98)00057-7, PII S0005272898000577
    • C.W. Hoganson, M.A. Pressler, D.A. Proshlyakov, G.T. Babcock, From water to oxygen and back again: mechanistic similarities in the enzymatic redox conversions between water and dioxygen, Biochim. Biophys. Acta 1365 (1998) 170-174. (Pubitemid 29359254)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1365 , Issue.1-2 , pp. 170-174
    • Hoganson, C.W.1    Pressler, M.A.2    Proshlyakov, D.A.3    Babcock, G.T.4
  • 299
    • 0033539481 scopus 로고    scopus 로고
    • How oxygen is activated and reduced in respiration
    • G. Babcock, How oxygen is activated and reduced in respiration, Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 12971-12973.
    • (1999) Proc. Natl. Acad. Sci. U. S. A , vol.96 , pp. 12971-12973
    • Babcock, G.1
  • 300
    • 80054728768 scopus 로고    scopus 로고
    • Photosynthetic water oxidation vs mitochondrial oxygen reduction: Distinct mechanistic parallels
    • T.P. Silverstein, Photosynthetic water oxidation vs. mitochondrial oxygen reduction: distinct mechanistic parallels, J. Bioenerg. Biomembr. 43 (2011) 437-446.
    • (2011) J. Bioenerg. Biomembr , vol.43 , pp. 437-446
    • Silverstein, T.P.1
  • 301
    • 0033576277 scopus 로고    scopus 로고
    • Cytochrome c oxidase: Catalytic cycle and mechanisms of proton pumping-A discussion
    • H. Michel, Cytochrome c oxidase: catalytic cycle and mechanisms of proton pumping-a discussion, Biochemistry 38 (1999) 15129-15140. (Pubitemid 129520343)
    • (1999) Biochemistry , vol.38 , Issue.46 , pp. 15129-15140
    • Michel, H.1
  • 302
    • 0038998833 scopus 로고    scopus 로고
    • Proton translocation by cytochrome c oxidase: A rejoinder to recent criticism
    • DOI 10.1021/bi9925322
    • M. Wikström, Proton translocation by cytochrome c oxidase a rejoiner to recent criticism, J. Am. Chem. Soc. 39 (2000) 3515-3519. (Pubitemid 30183831)
    • (2000) Biochemistry , vol.39 , Issue.13 , pp. 3515-3519
    • Wikstrom, M.1
  • 303
    • 0037056048 scopus 로고    scopus 로고
    • Proton translocation by cytochrome c oxidase in different phases of the catalytic cycle
    • DOI 10.1016/S0005-2728(02)00267-0, PII S0005272802002670
    • M. Wikstrom, M.I. Verkhovsky, Proton translocation by cytochrome c oxidase in different phases of the catalytic cycle, Biochim. Biophys. Acta 1555 (2002) 128-132. (Pubitemid 35246018)
    • (2002) Biochimica et Biophysica Acta - Bioenergetics , vol.1555 , Issue.1-3 , pp. 128-132
    • Wikstrom, M.1    Verkhovsky, M.I.2
  • 306
    • 33645732495 scopus 로고    scopus 로고
    • Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase
    • I. Belevich, M.I. Verkhovsky, M. Wikström, Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase, Nature 440 (2006) 829-832.
    • (2006) Nature , vol.440 , pp. 829-832
    • Belevich, I.1    Verkhovsky, M.I.2    Wikström, M.3
  • 307
    • 58049192387 scopus 로고    scopus 로고
    • The protonation state of the cross-linked tyrosine during the catalytic cycle of cytochrome c oxidase
    • E.A. Gorbikova, M. Wikstrom, M.I. Verkhovsky, The protonation state of the cross-linked tyrosine during the catalytic cycle of cytochrome c oxidase, J. Biol. Chem. 283 (2008) 34907-34912.
    • (2008) J. Biol. Chem , vol.283 , pp. 34907-34912
    • Gorbikova, E.A.1    Wikstrom, M.2    Verkhovsky, M.I.3
  • 308
    • 1542274547 scopus 로고    scopus 로고
    • Heme protein assemblies
    • C.J. Reedy, B.R. Gibney, Heme protein assemblies, Chem. Rev. 104 (2004) 617-649.
    • (2004) Chem. Rev , vol.104 , pp. 617-649
    • Reedy, C.J.1    Gibney, B.R.2
  • 309
    • 84884906575 scopus 로고
    • Electrostatic analysis of the midpoints of the four hemes in the bound cytochrome of the reaction center of Rp viridis
    • J. Jortner, B. Pullman (Eds.), Kluwer Academic Publisher, Dordrecht
    • M.R. Gunner, B. Honig, Electrostatic analysis of the midpoints of the four hemes in the bound cytochrome of the reaction center of Rp. viridis, in: J. Jortner, B. Pullman (Eds.), Perspectives in Photosynthesis: Proceedings of the Twenty-Second Jerusalem Symposium on Quantum Chemistry and Biochemistry, Kluwer Academic Publisher, Dordrecht, 1990, pp. 53-60.
    • (1990) Perspectives in Photosynthesis: Proceedings of the Twenty-Second Jerusalem Symposium on Quantum Chemistry and Biochemistry , pp. 53-60
    • Gunner, M.R.1    Honig, B.2
  • 310
    • 0001645795 scopus 로고    scopus 로고
    • Heme-peptide models for hemoproteins. 1. Solution chemistry of N-acetylmicroperoxidase-8
    • O.Q. Munro, H.M. Marques, Heme-peptide models for hemoproteins. 1. Solution chemistry of N-acetylmicroperoxidase-8, Inorg. Chem. 35 (1996) 3752-3767.
    • (1996) Inorg. Chem , vol.35 , pp. 3752-3767
    • Munro, O.Q.1    Marques, H.M.2
  • 311
    • 0000656480 scopus 로고    scopus 로고
    • Heme-peptide models for hemoproteins. 2. N-Acetylmicroperoxidase-8: Study of the φ-φ Dimers formed at high ionic strength using a modified version of molecular exciton theory
    • O.Q. Munro, H.M. Marques, Heme-peptide models for hemoproteins. 2. N-Acetylmicroperoxidase-8: Study of the φ-φ dimers formed at high ionic strength using a modified version of molecular exciton theory, Inorg. Chem. 35 (1996) 3768-3779.
    • (1996) Inorg. Chem , vol.35 , pp. 3768-3779
    • Munro, O.Q.1    Marques, H.M.2
  • 312
    • 0000259928 scopus 로고    scopus 로고
    • Coordination of N-donor ligands by the monomeric ferric porphyrin N-acetylmicroperoxidase-8
    • H.M. Marques, O.Q. Munro, T. Munro, M. de Wet, P.R. Vashi, Coordination of N-donor ligands by the monomeric ferric porphyrin N-acetylmicroperoxidase-8, Inorg. Chem. 38 (1999) 2312-2319.
    • (1999) Inorg. Chem , vol.38 , pp. 2312-2319
    • Marques, H.M.1    Munro, O.Q.2    Munro, T.3    De Wet, M.4    Vashi, P.R.5
  • 314
    • 4444247415 scopus 로고    scopus 로고
    • IINAcMP8)
    • DOI 10.1016/j.jinorgbio.2004.05.016, PII S0162013404001801
    • P.R. Vashi, H.M. Marques, The coordination of imidazole and substituted pyridines by the hemeoctapeptide N-acetyl-ferromicroperoxidase-8 (FeIINAcMP8), J. Inorg. Biochem. 98 (2004) 1471-1482. (Pubitemid 39165440)
    • (2004) Journal of Inorganic Biochemistry , vol.98 , Issue.9 , pp. 1471-1482
    • Vashi, P.R.1    Marques, H.M.2
  • 315
    • 33845278074 scopus 로고
    • Direct electrochemistry of the undacapeptide from cytochrome c (microperoxidase) at a glassy carbon electrode
    • R. Santucci, H. Reinhard, M. Brunori, Direct electrochemistry of the undacapeptide from cytochrome c (microperoxidase) at a glassy carbon electrode, J. Am. Chem. Soc. 110 (1988) 8536-8537.
    • (1988) J. Am. Chem. Soc , vol.110 , pp. 8536-8537
    • Santucci, R.1    Reinhard, H.2    Brunori, M.3
  • 316
    • 33745622986 scopus 로고    scopus 로고
    • as of hydroxyl ligands
    • DOI 10.1021/bi052182l
    • Y. Song, J. Mao, M.R. Gunner, Electrostatic environment of hemes in proteins: pKas of hydroxyl ligands, Biochemistry 45 (2006) 7949-7958. (Pubitemid 43996785)
    • (2006) Biochemistry , vol.45 , Issue.26 , pp. 7949-7958
    • Song, Y.1    Mao, J.2    Gunner, M.R.3
  • 319
    • 33645856788 scopus 로고    scopus 로고
    • On the status of ferryl protonation
    • R.K. Behan, M.T. Green, On the status of ferryl protonation, J. Inorg. Biochem. 100 (2006) 448-459.
    • (2006) J. Inorg. Biochem , vol.100 , pp. 448-459
    • Behan, R.K.1    Green, M.T.2
  • 320
    • 33244476516 scopus 로고    scopus 로고
    • Application of Badger's rule to heme and non-heme iron-oxygen bonds: An examination of ferryl protonation states
    • DOI 10.1021/ja054074s
    • M.T. Green, Application of Badger's rule to heme and non-heme iron-oxygen bonds: an examination of ferryl protonation states, J. Am. Chem. Soc. 128 (2006) 1902-1906. (Pubitemid 43277330)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.6 , pp. 1902-1906
    • Green, M.T.1
  • 322
    • 0033587483 scopus 로고    scopus 로고
    • Direct evidence for a tyrosine radical in the reaction of cytochrome c oxidase with hydrogen peroxide
    • DOI 10.1021/bi9911987
    • F. MacMillan, A. Kannt, J. Behr, T. Prisner, H. Michel, Direct evidence for a tyrosine radical in the reaction of cytochrome c oxidase with hydrogen peroxide, Biochemistry 38 (1999) 9179-9184. (Pubitemid 29347241)
    • (1999) Biochemistry , vol.38 , Issue.29 , pp. 9179-9184
    • MacMillan, F.1    Kannt, A.2    Behr, J.3    Prisner, T.4    Michel, H.5
  • 323
    • 0018118592 scopus 로고
    • Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • R. Richarz, K. Wüthrich, Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH, Biopolymers 17 (1975) 2133-2141. (Pubitemid 9015225)
    • (1978) Biopolymers , vol.17 , Issue.9 , pp. 2133-2141
    • Richarz, R.1    Wuthrich, K.2
  • 324
    • 0034654622 scopus 로고    scopus 로고
    • Insights into the functional role of the tyrosine-histidine linkage in cytochrome c oxidase [17]
    • DOI 10.1021/ja993774s
    • K.M. McCauley, J.M. Vrtis, J. Dupont, W.A. van der Donk, Insights into the functional role of the tyrosine-histidinde linkage in cytochrome c oxidase, J. Am. Chem. Soc. 122 (2000) 2403-2404. (Pubitemid 30164666)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.10 , pp. 2403-2404
    • McCauley, K.M.1    Vrtis, J.M.2    Dupont, J.3    Van Der Donk, W.A.4
  • 325
    • 0033514982 scopus 로고    scopus 로고
    • Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen
    • A. Jasaitis, M.I. Verkhovsky, J.E. Morgan, M.L. Verkhovskaya, M. Wikstrom, Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen, Biochemistry 38 (1999) 2697-2706.
    • (1999) Biochemistry , vol.38 , pp. 2697-2706
    • Jasaitis, A.1    Verkhovsky, M.I.2    Morgan, J.E.3    Verkhovskaya, M.L.4    Wikstrom, M.5
  • 326
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochrome c oxidase
    • DOI 10.1038/nature03921
    • K. Faxen, G. Gilderson, P. Adelroth, P. Brzezinski, A mechanistic principle for proton pumping by cytochrome c oxidase, Nature 437 (2005) 286-289. (Pubitemid 41294494)
    • (2005) Nature , vol.437 , Issue.7056 , pp. 286-289
    • Faxen, K.1    Gilderson, G.2    Adelroth, P.3    Brzezinski, P.4
  • 327
    • 33748885262 scopus 로고    scopus 로고
    • Towards the mechanism of proton pumping by the haem-copper oxidases
    • DOI 10.1016/j.bbabio.2006.01.010, PII S0005272806000235
    • M. Wikstrom, M.I. Verkhovsky, Towards the mechanism of proton pumping by the haem-copper oxidases, Biochim. Biophys. Acta 1757 (2006) 1047-1051. (Pubitemid 44427754)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.8 , pp. 1047-1051
    • Wikstrom, M.1    Verkhovsky, M.I.2
  • 328
    • 0039840998 scopus 로고    scopus 로고
    • Effects of mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeroides
    • DOI 10.1021/bi971458p
    • S. Jünemann, B. Meunier, R.B. Gennis, P.R. Rich, Effects of mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeroides, Biochemistry 36 (1997) 14456-14464. (Pubitemid 27509938)
    • (1997) Biochemistry , vol.36 , Issue.47 , pp. 14456-14464
    • Junemann, S.1    Meunier, B.2    Gennis, R.B.3    Rich, P.R.4
  • 329
    • 0030745897 scopus 로고    scopus 로고
    • The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer
    • A.A. Konstantinov, S. Siletsky, D. Mitchell, A. Kaulen, R.B. Gennis, The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer, Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 9085-9090.
    • (1997) Proc. Natl. Acad. Sci. U. S. A , vol.94 , pp. 9085-9090
    • Konstantinov, A.A.1    Siletsky, S.2    Mitchell, D.3    Kaulen, A.4    Gennis, R.B.5
  • 330
    • 0032478167 scopus 로고    scopus 로고
    • 2
    • DOI 10.1021/bi971877m
    • D. Zaslavsky, R.B. Gennis, Substitution of lysine-362 in a putative protonconducting channel in the cytochrome c oxidase from Rhodobacter sphaeroides blocks turnover with O2 but not with H2O2, Biochemistry 37 (1998) 3062-3067. (Pubitemid 28145760)
    • (1998) Biochemistry , vol.37 , Issue.9 , pp. 3062-3067
    • Zaslavsky, D.1    Gennis, R.B.2
  • 333
    • 57049130390 scopus 로고    scopus 로고
    • A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases
    • M.A. Sharpe, S. Ferguson-Miller, A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases, J. Bioenerg. Biomembr. 40 (2008) 541-549.
    • (2008) J. Bioenerg. Biomembr , vol.40 , pp. 541-549
    • Sharpe, M.A.1    Ferguson-Miller, S.2
  • 334
  • 336
    • 49349116297 scopus 로고    scopus 로고
    • Theoretical and computational analysis of the membrane potential generated by cytochrome c oxidase upon single electron injection into the enzyme
    • R. Sugitani, E.S. Medvedev, A.A. Stuchebrukhov, Theoretical and computational analysis of the membrane potential generated by cytochrome c oxidase upon single electron injection into the enzyme, Biochim. Biophys. Acta 1777 (2008) 1129-1139.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1129-1139
    • Sugitani, R.1    Medvedev, E.S.2    Stuchebrukhov, A.A.3
  • 338
    • 79751528117 scopus 로고    scopus 로고
    • Exploration of the cytochrome c oxidase pathway puzzle and examination of the origin of elusive mutational effects
    • S. Chakrabarty, I. Namslauer, P. Brzezinski, A. Warshel, Exploration of the cytochrome c oxidase pathway puzzle and examination of the origin of elusive mutational effects, Biochim. Biophys. Acta 1807 (2011) 413-426.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 413-426
    • Chakrabarty, S.1    Namslauer, I.2    Brzezinski, P.3    Warshel, A.4
  • 339
    • 64849103999 scopus 로고    scopus 로고
    • Microscopic pKa analysis of Glu286 in cytochrome c oxidase (Rhodobacter sphaeroides): Toward a calibrated molecular model
    • N. Ghosh, X. Prat-Resina, M.R. Gunner, Q. Cui, Microscopic pKa analysis of Glu286 in cytochrome c oxidase (Rhodobacter sphaeroides): toward a calibrated molecular model, Biochemistry 48 (2009) 2468-2485.
    • (2009) Biochemistry , vol.48 , pp. 2468-2485
    • Ghosh, N.1    Prat-Resina, X.2    Gunner, M.R.3    Cui, Q.4
  • 340
    • 33746652164 scopus 로고    scopus 로고
    • + conduction in the D-pathway of Cytochrome c Oxidase: A study of the wild type and N98D mutant enzymes
    • DOI 10.1016/j.bbabio.2006.05.028, PII S0005272806001642
    • J. Xu, G.A. Voth, Free energy profiles for H+ conduction in the D-pathway of cytochrome c oxidase: a study of the wild type and N98D mutant enzymes, Biochim. Biophys. Acta 1757 (2006) 852-859. (Pubitemid 44150607)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.7 , pp. 852-859
    • Xu, J.1    Voth, G.A.2
  • 341
    • 38749152834 scopus 로고    scopus 로고
    • Redox-coupled proton pumping in cytochrome c oxidase: Further insights from computer simulation
    • J. Xu, G.A. Voth, Redox-coupled proton pumping in cytochrome c oxidase: further insights from computer simulation, Biochim. Biophys. Acta 1777 (2008) 196-201.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 196-201
    • Xu, J.1    Voth, G.A.2
  • 342
    • 84855943335 scopus 로고    scopus 로고
    • Insights into the mechanism of proton transport in cytochrome c oxidase
    • T. Yamashita, G.A. Voth, Insights into the mechanism of proton transport in cytochrome c oxidase, J. Am. Chem. Soc. 134 (2012) 1147-1152.
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 1147-1152
    • Yamashita, T.1    Voth, G.A.2
  • 343
    • 33947285426 scopus 로고    scopus 로고
    • Exploring pathways and barriers for coupled ET/PT in cytochrome c oxidase: A general framework for examining energetics and mechanistic alternatives
    • DOI 10.1016/j.bbabio.2007.01.015, PII S0005272807000199
    • M. Olsson, P. Siegbahn, M. Blomberg, A. Warshel, Exploring pathways and barriers for coupled ET/PT in cytochrome c oxidase: a general framework for examining energetics and mechanistic alternatives, Biochim. Biophys. Acta 1767 (2007) 244-260. (Pubitemid 46420433)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.3 , pp. 244-260
    • Olsson, M.H.M.1    Siegbahn, P.E.M.2    Blomberg, M.R.A.3    Warshel, A.4
  • 344
    • 33646268674 scopus 로고    scopus 로고
    • Monte Carlo simulations of proton pumps: On the working principles of the biological valve that controls proton pumping in cytochrome c oxidase
    • M.H.M. Olsson, A. Warshel, Monte Carlo simulations of proton pumps: on the working principles of the biological valve that controls proton pumping in cytochrome c oxidase, Proc. Natl. Acad. Sci. 103 (2006) 6500-6505.
    • (2006) Proc. Natl. Acad. Sci , vol.103 , pp. 6500-6505
    • Olsson, M.H.M.1    Warshel, A.2
  • 345
    • 84857913911 scopus 로고    scopus 로고
    • Proton-pumping mechanism of cytochrome c oxidase: A kinetic master-equation approach
    • Y.C. Kim, G. Hummer, Proton-pumping mechanism of cytochrome c oxidase: a kinetic master-equation approach, Biochim. Biophys. Acta 1817 (2012) 526-536.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 526-536
    • Kim, Y.C.1    Hummer, G.2
  • 347
    • 80052475923 scopus 로고    scopus 로고
    • Glu-286 rotation and water wire reorientation are unlikely the gating elements for proton pumping in cytochrome c oxidase
    • S. Yang, Q. Cui, Glu-286 rotation and water wire reorientation are unlikely the gating elements for proton pumping in cytochrome c oxidase, Biophys. J. 101 (2011) 61-69.
    • (2011) Biophys. J , vol.101 , pp. 61-69
    • Yang, S.1    Cui, Q.2
  • 348
    • 78249242740 scopus 로고    scopus 로고
    • The identity of the transient proton loading site of the proton-pumping mechanism of cytochrome c oxidase
    • V.R. Kaila, V. Sharma, M. Wikstrom, The identity of the transient proton loading site of the proton-pumping mechanism of cytochrome c oxidase, Biochim. Biophys. Acta 1807 (2011) 80-84.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 80-84
    • Kaila, V.R.1    Sharma, V.2    Wikstrom, M.3
  • 349
    • 58149147161 scopus 로고    scopus 로고
    • Proton pumping mechanism in cytochrome c oxidase
    • P.E. Siegbahn, M.R. Blomberg, Proton pumping mechanism in cytochrome c oxidase, J. Phys. Chem. A 112 (2008) 12772-12780.
    • (2008) J. Phys. Chem. A , vol.112 , pp. 12772-12780
    • Siegbahn, P.E.1    Blomberg, M.R.2
  • 350
    • 84857922147 scopus 로고    scopus 로고
    • Design of photoactive ruthenium complexes to study electron transfer and proton pumping in cytochrome oxidase
    • B. Durham, F. Millett, Design of photoactive ruthenium complexes to study electron transfer and proton pumping in cytochrome oxidase, Biochim. Biophys. Acta 1817 (2012) 567-574.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 567-574
    • Durham, B.1    Millett, F.2
  • 351
    • 0032487395 scopus 로고    scopus 로고
    • Factors determining electron-transfer rates in cytochrome c oxidase: Investigation of the oxygen reaction in the R sphaeroides enzyme
    • DOI 10.1016/S0005-2728(98)00142-X, PII S000527289800142X
    • P. Adelroth, M. Ek, P. Brzezinski, Factors determining electron-transfer rates in cytochrome c oxidase: investigation of the oxygen reaction in the R. sphaeroides enzyme, Biochim. Biophys. Acta 1367 (1998) 107-117. (Pubitemid 28451587)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1367 , Issue.1-3 , pp. 107-117
    • Adelroth, P.1    Ek, M.2    Brzezinski, P.3
  • 352
    • 0034663652 scopus 로고    scopus 로고
    • Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochrome c oxidase
    • DOI 10.1016/S0005-2728(00)00194-8, PII S0005272800001948
    • P. Ådelroth, M. Karpeforsa, G. Gildersona, F.L. Tomsonc, R.B. Gennis, P. Brzezinski, Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochrome c oxidase, Biochim. Biophys. Acta 1459 (2000) 533-539. (Pubitemid 30612430)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1459 , Issue.2-3 , pp. 533-539
    • Adelroth, P.1    Karpefors, M.2    Gilderson, G.3    Tomson, F.L.4    Gennis, R.B.5    Brzezinski, P.6
  • 353
    • 80051588632 scopus 로고    scopus 로고
    • The D-channel of cytochrome oxidase: An alternative view
    • M. Wikström, M.I. Verkhovsky, The D-channel of cytochrome oxidase: an alternative view, Biochim. Biophys. Acta 1807 (2011) 1273-1278.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1273-1278
    • Wikström, M.1    Verkhovsky, M.I.2
  • 354
    • 67649986251 scopus 로고    scopus 로고
    • Mechanism and energetics by which glutamic acid 242 prevents leaks in cytochrome c oxidase
    • V.R. Kaila, M.I. Verkhovsky, G. Hummer, M. Wikström, Mechanism and energetics by which glutamic acid 242 prevents leaks in cytochrome c oxidase, Biochim. Biophys. Acta 1787 (2009) 1205-1214.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1205-1214
    • Kaila, V.R.1    Verkhovsky, M.I.2    Hummer, G.3    Wikström, M.4
  • 357
    • 0032311173 scopus 로고    scopus 로고
    • Structure and dynamics of a proton shuttle in cytochrome c oxidase
    • R. Pomes, G. Hummer, M. Wikstrom, Structure and dynamics of a proton shuttle in cytochrome c oxidase, Biochim. Biophys. Acta 1365 (1999) 255-260.
    • (1999) Biochim. Biophys. Acta , vol.1365 , pp. 255-260
    • Pomes, R.1    Hummer, G.2    Wikstrom, M.3
  • 358
    • 33748895869 scopus 로고    scopus 로고
    • Combined DFT and electrostatics study of the proton pumping mechanism in cytochrome c oxidase
    • DOI 10.1016/j.bbabio.2005.12.003, PII S0005272805002793
    • J. Quenneville, D.M. Popovic, A.A. Stuchebrukhov, Combined DFT and electrostatics study of the proton pumping mechanism in cytochrome c oxidase, Biochim. Biophys. Acta 1757 (2006) 1035-1046. (Pubitemid 44427750)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.8 , pp. 1035-1046
    • Quenneville, J.1    Popovic, D.M.2    Stuchebrukhov, A.A.3
  • 359
    • 84857916864 scopus 로고    scopus 로고
    • Coupled electron and proton transfer reactions during the O → e transition in bovine cytochrome c oxidase
    • D.M. Popovic, A.A. Stuchebrukhov, Coupled electron and proton transfer reactions during the O → E transition in bovine cytochrome c oxidase, Biochim. Biophys. Acta 1817 (2012) 506-517.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 506-517
    • Popovic, D.M.1    Stuchebrukhov, A.A.2
  • 360
    • 63449091255 scopus 로고    scopus 로고
    • Functional hydration and conformational gating of proton uptake in cytochrome c oxidase
    • R.M. Henry, C.H. Yu, T. Rodinger, R. Pomes, Functional hydration and conformational gating of proton uptake in cytochrome c oxidase, J. Mol. Biol. 387 (2009) 1165-1185.
    • (2009) J. Mol. Biol , vol.387 , pp. 1165-1185
    • Henry, R.M.1    Yu, C.H.2    Rodinger, T.3    Pomes, R.4
  • 361
    • 79957871568 scopus 로고    scopus 로고
    • Molecular basis of proton uptake in single and double mutants of cytochrome c oxidase
    • R.M. Henry, D. Caplan, E. Fadda, R. Pomes, Molecular basis of proton uptake in single and double mutants of cytochrome c oxidase, J. Phys. Condens. Matter 23 (2011) 234102.
    • (2011) J. Phys. Condens. Matter , vol.23 , pp. 234102
    • Henry, R.M.1    Caplan, D.2    Fadda, E.3    Pomes, R.4
  • 363
    • 10044290841 scopus 로고    scopus 로고
    • Redox-dependent pKa of CuB histidine ligand in cytochrome c oxidase
    • J. Quenneville, D.M. Popovic, A.A. Stuchebrukhov, Redox-dependent pKa of CuB histidine ligand in cytochrome c oxidase, J. Phys. Chem. B 108 (2004) 18383-18389.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 18383-18389
    • Quenneville, J.1    Popovic, D.M.2    Stuchebrukhov, A.A.3
  • 364
    • 78650545848 scopus 로고    scopus 로고
    • Proton-coupled electron transfer in cytochrome oxidase
    • V.R. Kaila, M.I. Verkhovsky, M. Wikström, Proton-coupled electron transfer in cytochrome oxidase, Chem. Rev. 110 (2010) 7062-7081.
    • (2010) Chem. Rev , vol.110 , pp. 7062-7081
    • Kaila, V.R.1    Verkhovsky, M.I.2    Wikström, M.3
  • 366
    • 0030894333 scopus 로고    scopus 로고
    • The importance of the protein in controlling the electrochemistry of heme metalloproteins: Methods of calculation and analysis
    • DOI 10.1007/s007750050116
    • M.R. Gunner, E. Alexov, E. Torres, S. Lipovaca, The importance of the protein in controlling the electrochemistry of heme metalloproteins: methods of calculation and analysis, J. Biol. Inorg. Chem. 2 (1997) 126-134. (Pubitemid 27161110)
    • (1997) Journal of Biological Inorganic Chemistry , vol.2 , Issue.1 , pp. 126-134
    • Gunner, M.R.1    Alexov, E.2    Torres, E.3    Lipovaca, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.