메뉴 건너뛰기




Volumn 586, Issue 5, 2012, Pages 603-616

Back-reactions, short-circuits, leaks and other energy wasteful reactions in biological electron transfer: Redox tuning to survive life in O 2

Author keywords

Bioenergetics; Cytochrome b c1 and b 6f; Electron transfer; Evolution; Oxidative stress; Photosystem; Protective reactions; Reactive oxygen species (ROS)

Indexed keywords

DIPEPTIDYL CARBOXYPEPTIDASE; HETERODIMER; OXYGEN; REACTIVE OXYGEN METABOLITE;

EID: 84857921513     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.12.039     Document Type: Review
Times cited : (211)

References (138)
  • 1
    • 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
  • 2
    • 0023759565 scopus 로고
    • The potential diagram for oxygen at pH 7
    • P.M. Wood The potential diagram for oxygen at pH 7 Biochem. J. 253 1988 287 289
    • (1988) Biochem. J. , vol.253 , pp. 287-289
    • Wood, P.M.1
  • 3
    • 71849095133 scopus 로고    scopus 로고
    • Cause and consequence. mitochondrial dysfunction initiates and propagates neuronal dysfunction, neuronal death and behavioral abnormalities in age-associated neurodegenerative diseases
    • G.E. Gibson, A. Starkov, J.P. Blass, R.R. Ratan, and M.F. Beal Cause and consequence. mitochondrial dysfunction initiates and propagates neuronal dysfunction, neuronal death and behavioral abnormalities in age-associated neurodegenerative diseases Biochim. Biophys. Acta 1802 2010 122 134
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 122-134
    • Gibson, G.E.1    Starkov, A.2    Blass, J.P.3    Ratan, R.R.4    Beal, M.F.5
  • 4
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • T. Finkel Signal transduction by reactive oxygen species J. Cell Biol. 194 2011 7 15
    • (2011) J. Cell Biol. , vol.194 , pp. 7-15
    • Finkel, T.1
  • 7
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution
    • DOI 10.1038/318618a0
    • J. Deisenhofer, O. Epp, K. Miki, R. Huber, and H. Michel Structure of the protein subunit in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 A resolution Nature 318 1985 618 624 (Pubitemid 16172409)
    • (1985) Nature , vol.318 , Issue.6047 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3
  • 8
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobaoterial photosystem I at 2.5 Å resolution
    • DOI 10.1038/35082000
    • P. Jordan, P. Fromme, H.T. Witt, O. Klukas, W. Saenger, and N. Krauss Three-dimensional structure of cyanobacterial photosystem I at 2.5 A resolution Nature 411 2001 909 917 (Pubitemid 32601481)
    • (2001) Nature , vol.411 , Issue.6840 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 9
    • 0032548142 scopus 로고    scopus 로고
    • Three-dimensional structure of the plant photosystem II reaction centre at 8 Å resolution
    • DOI 10.1038/24421
    • K.-H. Rhee, E.P. Morris, J. Barber, and W. Kühlbrandt Three-dimensional structure of the plant photosystem II reaction centre at 8 A resolution Nature 396 1998 283 286 (Pubitemid 28541395)
    • (1998) Nature , vol.396 , Issue.6708 , pp. 283-286
    • Rhee, K.-H.1    Morris, E.P.2    Barber, J.3    Kuhlbrandt, W.4
  • 10
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • DOI 10.1038/35055589
    • A. Zouni, H.T. Witt, J. Kern, P. Fromme, N. Krauss, W. Saenger, and P. Orth Crystal structure of Photosystem II from Synechococcus elongatus at 3.8 resolution Nature 409 2001 739 743 (Pubitemid 32144521)
    • (2001) Nature , vol.409 , Issue.6821 , pp. 739-743
    • Zouni, A.1    Witt, H.-T.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6    Orth, P.7
  • 11
    • 0348148910 scopus 로고    scopus 로고
    • Crystal structure of plant photosystem I
    • DOI 10.1038/nature02200
    • A. Ben-Shem, F. Frolow, and N. Nelson Crystal structure of plant photosystem I Nature 426 2003 630 635 (Pubitemid 38009364)
    • (2003) Nature , vol.426 , Issue.6967 , pp. 630-635
    • Ben-Shem, A.1    Frolow, F.2    Nelson, N.3
  • 12
    • 0025885119 scopus 로고
    • Photosynthetic reaction centres: Variations on a common structural theme?
    • W. Nitschke, and A.W. Rutherford Photosynthetic reaction centres: 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
  • 13
    • 0017392514 scopus 로고
    • Kinetics of electron transfer between the primary and the secondary electron acceptor in reaction centers from Rhodopseudomonas sphaeroides
    • A. Vermeglio, and R.K. Clayton Kinetics of electron transfer between the primary and the secondary electron acceptor in reaction centers from Rhodopseudomonas 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
  • 14
    • 0031015412 scopus 로고    scopus 로고
    • Electron transfer and arrangement of the redox cofactors in photosystem I
    • DOI 10.1016/S0005-2728(96)00112-0, PII S0005272896001120
    • K. Brettel Electron transfer and arrangement of the redox cofactors in photosystem I Biochim. Biophys. Acta 1318 1997 322 373 (Pubitemid 27073613)
    • (1997) Biochimica et Biophysica Acta - Bioenergetics , vol.1318 , Issue.3 , pp. 322-373
    • Brettel, K.1
  • 15
    • 0010884753 scopus 로고
    • On the theory of oxidation-reduction reactions involving electron transfer
    • R.A. Marcus On the theory of oxidation-reduction reactions involving electron transfer J. Chem. Phys. 24 1956 966 978
    • (1956) J. Chem. Phys. , vol.24 , pp. 966-978
    • Marcus, R.A.1
  • 16
    • 0002096235 scopus 로고    scopus 로고
    • Outline of theory of protein electron transfer
    • D.S. Bendall, BIOS Scientific Publishers Oxford
    • C.C. Moser, and P.L. Dutton Outline of theory of protein electron transfer D.S. Bendall, Protein electron transfer 1996 BIOS Scientific Publishers Oxford 1 21
    • (1996) Protein Electron Transfer , pp. 1-21
    • Moser, C.C.1    Dutton, P.L.2
  • 19
    • 34547108335 scopus 로고    scopus 로고
    • Heliobacterial photosynthesis
    • DOI 10.1007/s11120-007-9162-4
    • M. Heinnickel, and J.H. Golbeck Heliobacterial photosynthesis Photosynth. Res. 92 2007 35 53 (Pubitemid 47101223)
    • (2007) Photosynthesis Research , vol.92 , Issue.1 , pp. 35-53
    • Heinnickel, M.1    Golbeck, J.H.2
  • 20
    • 33847634723 scopus 로고    scopus 로고
    • B in Heliobacterium modesticaldum
    • DOI 10.1021/bi0622165
    • M. Heinnickel, G. Shen, and J.H. Golbeck Identification and characterization of PshB, the dicluster ferredoxin that harbors the terminal electron acceptors F(A) and F(B) in Heliobacterium modesticaldum Biochemistry 46 2007 2530 2536 (Pubitemid 46362426)
    • (2007) Biochemistry , vol.46 , Issue.9 , pp. 2530-2536
    • Heinnickel, M.1    Shen, G.2    Golbeck, J.H.3
  • 21
    • 0025366169 scopus 로고
    • Photosynthetic reaction center of green sulfur bacteria studied by EPR
    • DOI 10.1021/bi00468a005
    • W. Nitschke, U. Feiler, and A.W. Rutherford Photosynthetic reaction center of green sulfur bacteria studied by EPR Biochemistry 29 1990 3834 3842 (Pubitemid 20151292)
    • (1990) Biochemistry , vol.29 , Issue.16 , pp. 3834-3842
    • Nitschke, W.1    Feiler, U.2    Rutherford, A.W.3
  • 23
    • 1942436332 scopus 로고    scopus 로고
    • Evolution of photosystem I - From symmetry through pseudosymmetry to asymmetry
    • DOI 10.1016/S0014-5793(04)00360-6, PII S0014579304003606
    • A. Ben-Shem, F. Frolow, and N. Nelson Evolution of photosystem I - from symmetry through pseudo-symmetry to asymmetry FEBS Lett. 564 2004 274 280 (Pubitemid 38520933)
    • (2004) FEBS Letters , vol.564 , Issue.3 , pp. 274-280
    • Ben-Shem, A.1    Frolow, F.2    Nelson, N.3
  • 24
    • 0035976011 scopus 로고    scopus 로고
    • Electron transfer in photosystem I
    • DOI 10.1016/S0005-2728(01)00202-X, PII S000527280100202X
    • K. Brettel, and W. Leibl Electron transfer in photosystem I Biochim. Biophys. Acta 1507 2001 100 114 (Pubitemid 33001515)
    • (2001) Biochimica et Biophysica Acta - Bioenergetics , vol.1507 , Issue.1-3 , pp. 100-114
    • Brettel, K.1    Leibl, W.2
  • 25
    • 67649460705 scopus 로고    scopus 로고
    • Protein-cofactor interactions in bioenergetic complexes: The role of the A1A and A1B phylloquinones in Photosystem i
    • N. Srinivasan, and J.H. Golbeck Protein-cofactor interactions in bioenergetic complexes: the role of the A1A and A1B phylloquinones in Photosystem I Biochim. Biophys. Acta 1787 2009 1057 1088
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1057-1088
    • Srinivasan, N.1    Golbeck, J.H.2
  • 26
    • 77956520951 scopus 로고    scopus 로고
    • The production and scavenging of reactive oxygen species in the plastoquinone pool of chloroplast thylakoid membranes
    • M.M. Mubarakshina, and B.N. Ivanov The production and scavenging of reactive oxygen species in the plastoquinone pool of chloroplast thylakoid membranes Physiol Plant 140 2010 103 110
    • (2010) Physiol Plant , vol.140 , pp. 103-110
    • Mubarakshina, M.M.1    Ivanov, B.N.2
  • 27
    • 63449114738 scopus 로고    scopus 로고
    • Breaking biological symmetry in membrane proteins: The asymmetrical orientation of PsaC on the pseudo-C2 symmetric Photosystem i core
    • B. Jagannathan, and J.H. Golbeck Breaking biological symmetry in membrane proteins: the asymmetrical orientation of PsaC on the pseudo-C2 symmetric Photosystem I core Cell Mol. Life Sci. 66 2009 1257 1270
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 1257-1270
    • Jagannathan, B.1    Golbeck, J.H.2
  • 28
    • 0037047381 scopus 로고    scopus 로고
    • PGR5 is involved in cyclic electron flow around photosystem i and is essential for photoprotection in Arabidopsis
    • Y. Munekage, M. Hojo, J. Meurer, T. Endo, M. Tasaka, and T. Shikanai PGR5 is involved in cyclic electron flow around photosystem I and is essential for photoprotection in Arabidopsis Cell 110 2002 361 371
    • (2002) Cell , vol.110 , pp. 361-371
    • Munekage, Y.1    Hojo, M.2    Meurer, J.3    Endo, T.4    Tasaka, M.5    Shikanai, T.6
  • 29
    • 38749133045 scopus 로고    scopus 로고
    • A complex containing PGRL1 and PGR5 is involved in the switch between linear and cyclic electron flow in Arabidopsis
    • G. DalCorso A complex containing PGRL1 and PGR5 is involved in the switch between linear and cyclic electron flow in Arabidopsis Cell 132 2008 273 285
    • (2008) Cell , vol.132 , pp. 273-285
    • Dalcorso, G.1
  • 30
    • 77951622488 scopus 로고    scopus 로고
    • Isolation of the elusive supercomplex that drives cyclic electron flow in photosynthesis
    • M. Iwai, K. Takizawa, R. Tokutsu, A. Okamuro, Y. Takahashi, and J. Minagawa Isolation of the elusive supercomplex that drives cyclic electron flow in photosynthesis Nature 464 2010 1210 1213
    • (2010) Nature , vol.464 , pp. 1210-1213
    • Iwai, M.1    Takizawa, K.2    Tokutsu, R.3    Okamuro, A.4    Takahashi, Y.5    Minagawa, J.6
  • 31
    • 0033600564 scopus 로고    scopus 로고
    • In vivo analysis of the electron transfer within photosystem I: Are the two phylloquinones involved?
    • P. Joliot, and A. Joliot In vivo analysis of the electron transfer within photosystem I: are the two phylloquinones involved? Biochemistry 38 1999 11130 11136
    • (1999) Biochemistry , vol.38 , pp. 11130-11136
    • Joliot, P.1    Joliot, A.2
  • 33
    • 21244447030 scopus 로고    scopus 로고
    • Biochemical and biophysical characterization of photosystem I from phytoene desaturase and ζ-carotene desaturase deletion mutants of Synechocystis Sp. PCC 6803: Evidence for PsaA- and PsaB-side electron transport in cyanobacteria
    • DOI 10.1074/jbc.M500809200
    • J.A. Bautista, F. Rappaport, M. Guergova-Kuras, R.O. Cohen, J.H. Golbeck, J.Y. Wang, D. Beal, and B.A. Diner Biochemical and biophysical characterization of photosystem I from phytoene desaturase and zeta-carotene desaturase deletion mutants of Synechocystis Sp. PCC 6803: evidence for PsaA- and PsaB-side electron transport in cyanobacteria J. Biol. Chem. 280 2005 20030 20041 (Pubitemid 41379532)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.20 , pp. 20030-20041
    • Bautista, J.A.1    Rappaport, F.2    Guergova-Kuras, M.3    Cohen, R.O.4    Golbeck, J.H.5    Wang, J.Y.6    Beal, D.7    Diner, B.A.8
  • 34
    • 33745030538 scopus 로고    scopus 로고
    • -] radical pair of photosystem I indicates that both reaction center subunits are competent in electron transfer in cyanobacteria, green algae, and higher plants
    • DOI 10.1021/bi060330h
    • S. Santabarbara, I. Kuprov, P.J. Hore, A. Casal, P. Heathcote, and M.C. Evans Analysis of the spin-polarized electron spin echo of the [P700+ A1-] radical pair of photosystem I indicates that both reaction center subunits are competent in electron transfer in cyanobacteria, green algae, and higher plants Biochemistry 45 2006 7389 7403 (Pubitemid 43877425)
    • (2006) Biochemistry , vol.45 , Issue.23 , pp. 7389-7403
    • Santabarbara, S.1    Kuprov, I.2    Hore, P.J.3    Casal, A.4    Heathcote, P.5    Evans, M.C.W.6
  • 35
    • 0346732319 scopus 로고    scopus 로고
    • Redox Potential of Quinones in Both Electron Transfer Branches of Photosystem I
    • DOI 10.1074/jbc.M306434200
    • H. Ishikita, and E.W. Knapp Redox potential of quinones in both electron transfer branches of photosystem I J. Biol. Chem. 278 2003 52002 52011 (Pubitemid 38035785)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.52 , pp. 52002-52011
    • Ishikita, H.1    Knapp, E.-W.2
  • 36
    • 0037453370 scopus 로고    scopus 로고
    • 1 in photosystem I: Only the slower phase is activated
    • DOI 10.1016/S0005-2728(03)00024-0
    • R. Agalarov, and K. Brettel Temperature dependence of biphasic forward electron transfer from the phylloquinone(s) A1 in photosystem I: only the slower phase is activated Biochim. Biophys. Acta 1604 2003 7 12 (Pubitemid 36398471)
    • (2003) Biochimica et Biophysica Acta - Bioenergetics , vol.1604 , Issue.1 , pp. 7-12
    • Agalarov, R.1    Brettel, K.2
  • 37
    • 21944440651 scopus 로고    scopus 로고
    • X
    • DOI 10.1016/j.bbabio.2005.05.001, PII S0005272805001155
    • S. Santabarbara, P. Heathcote, and M.C. Evans Modelling of the electron transfer reactions in Photosystem I by electron tunnelling theory: The phylloquinones bound to the PsaA and the PsaB reaction centre subunits of PS I are almost isoenergetic to the iron-sulfur cluster F(X) Biochim. Biophys. Acta 1708 2005 283 310 (Pubitemid 40949558)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1708 , Issue.3 , pp. 283-310
    • Santabarbara, S.1    Heathcote, P.2    Evans, M.C.W.3
  • 38
    • 0018529528 scopus 로고
    • Triplet states in photosystem 1 of spinach chloroplasts and subchloroplast particles
    • H.A. Frank, M.B. McLean, and K. Sauer Triplet states in photosystem 1 of spinach chloroplasts and subchloroplast particles Proc. Natl. Acad. Sci. USA 76 1979 5124 5128
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 5124-5128
    • Frank, H.A.1    McLean, M.B.2    Sauer, K.3
  • 39
    • 0019879096 scopus 로고
    • Reaction center triplet states in photosystem i and photosystem II
    • A.W. Rutherford, and J.E. Mullet Reaction center triplet states in photosystem I and photosystem II Biochim. Biophys. Acta 635 1981 225 235
    • (1981) Biochim. Biophys. Acta , vol.635 , pp. 225-235
    • Rutherford, A.W.1    Mullet, J.E.2
  • 41
    • 79960560731 scopus 로고    scopus 로고
    • Modeling Photosystem i with the alternative reaction center protein PsaB2 in the nitrogen fixing cyanobacterium Nostoc punctiforme
    • A. Magnuson, H. Krassen, K. Stensjo, F.M. Ho, and S. Styring Modeling Photosystem I with the alternative reaction center protein PsaB2 in the nitrogen fixing cyanobacterium Nostoc punctiforme Biochim. Biophys. Acta 1807 2011 1152 1161
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1152-1161
    • Magnuson, A.1    Krassen, H.2    Stensjo, K.3    Ho, F.M.4    Styring, S.5
  • 43
    • 38049011376 scopus 로고    scopus 로고
    • 4Ca cluster and to the evolution of molecular oxygen in Photosystem II
    • 4Ca 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
  • 44
    • 0345471070 scopus 로고    scopus 로고
    • A ubiquinone
    • DOI 10.1016/S0014-5793(03)00270-9
    • M.C. Wakeham, M.G. Goodwin, C. McKibbin, and M.R. Jones Photo-accumulation of the P+QB- radical pair state in purple bacterial reaction centres that lack the QA ubiquinone FEBS Lett. 540 2003 234 240 (Pubitemid 36398063)
    • (2003) FEBS Letters , vol.540 , Issue.1-3 , pp. 234-240
    • Wakeham, M.C.1    Goodwin, M.G.2    McKibbin, C.3    Jones, M.R.4
  • 46
    • 82755181814 scopus 로고    scopus 로고
    • Charge separation in Photosystem II: A comparative and evolutionary overview
    • T. Cardona, A. Sedoud, N. Cox, and 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
  • 47
    • 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, and 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
  • 48
    • 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, and 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
  • 49
    • 0023048040 scopus 로고
    • Radical-pair energetics and decay mechanisms in reaction centers containing anthraquinones, naphthoquinones of benzoquinones in place of ubiquinone
    • N.W. Woodbury, W.W. Parson, M.R. Gunner, R.C. Prince, and P.L. Dutton Radical-pair energetics and decay mechanisms in reaction centers containing anthraquinones, naphthoquinones of benzoquinones in place of ubiquinone Biochim. Biophys. Acta 851 1986 6 22
    • (1986) Biochim. Biophys. Acta , vol.851 , pp. 6-22
    • Woodbury, N.W.1    Parson, W.W.2    Gunner, M.R.3    Prince, R.C.4    Dutton, P.L.5
  • 50
    • 0022104260 scopus 로고
    • The effect of an applied electric field on the charge recombination kinetics in reaction centers reconstituted in planar lipid bilayers
    • A. Gopher, Y. Blatt, M. Schönfeld, M.Y. Okamura, and G. Feher The effect of an applied electric field on the charge recombination kinetics in reaction centers reconstituted in planar lipid bilayers Biophys. J. 48 1985 311 320
    • (1985) Biophys. J. , vol.48 , pp. 311-320
    • Gopher, A.1    Blatt, Y.2    Schönfeld, M.3    Okamura, M.Y.4    Feher, G.5
  • 51
    • 84857914291 scopus 로고
    • Electron transfer reactions in reaction center protein from Rps. sphaeroides
    • M.R. Gunner, P.L. Dutton, N.W. Woodbury, and W.W. Parson Electron transfer reactions in reaction center protein from Rps. sphaeroides Biophys. J. 49 1986 A586
    • (1986) Biophys. J. , vol.49 , pp. 586
    • Gunner, M.R.1    Dutton, P.L.2    Woodbury, N.W.3    Parson, W.W.4
  • 52
    • 0003035415 scopus 로고
    • - recombination kinetics in reaction centers from Rhodopseudomonas viridis: The effect of pH and temperature
    • - recombination kinetics in reaction centers from Rhodopseudomonas viridis: the effect of pH and temperature Biochim. Biophys. Acta 974 1989 54 65
    • (1989) Biochim. Biophys. Acta , vol.974 , pp. 54-65
    • Sebban, P.1    Wraight, C.A.2
  • 54
    • 0019879108 scopus 로고
    • A light-induced spin-polarized triplet detected by EPR in photosystem II reaction centers
    • A.W. Rutherford, D.R. Paterson, and J.E. Mullet A light-induced spin-polarized triplet detected by EPR in photosystem II reaction centers Biochim. Biophys. Acta 635 1981 205 214
    • (1981) Biochim. Biophys. Acta , vol.635 , pp. 205-214
    • Rutherford, A.W.1    Paterson, D.R.2    Mullet, J.E.3
  • 56
    • 0002928340 scopus 로고
    • Electron transfer in photosystem II
    • H.J. van Gorkom Electron transfer in photosystem II Photosynth. Res. 6 1985 97 112
    • (1985) Photosynth. Res. , vol.6 , pp. 97-112
    • Van Gorkom, H.J.1
  • 58
    • 0038322621 scopus 로고    scopus 로고
    • Physical mechanisms of generation and deactivation of singlet oxygen
    • C. Schweitzer, and R. Schmidt Physical mechanisms of generation and deactivation of singlet oxygen Chem. Rev. 103 2003 1685 1757
    • (2003) Chem. Rev. , vol.103 , pp. 1685-1757
    • Schweitzer, C.1    Schmidt, R.2
  • 59
    • 18744409047 scopus 로고    scopus 로고
    • Singlet oxygen production in herbicide-treated photosystem II
    • DOI 10.1016/S0014-5793(02)03724-9, PII S0014579302037249
    • C. Fufezan, A.W. Rutherford, and A. Krieger-Liszkay Singlet oxygen production in herbicide-treated photosystem II FEBS Lett. 532 2002 407 410 (Pubitemid 35441382)
    • (2002) FEBS Letters , vol.532 , Issue.3 , pp. 407-410
    • Fufezan, C.1    Rutherford, A.W.2    Krieger-Liszkay, A.3
  • 60
    • 0000960124 scopus 로고
    • Kok's oxygen clock: What makes it tick? the structure of P680 and consequences of its oxidizing power
    • H.J. van Gorkom, and J.P.M. Schelvis Kok's oxygen clock: what makes it tick? The structure of P680 and consequences of its oxidizing power Photosynth. Res. 38 1993 297 301
    • (1993) Photosynth. Res. , vol.38 , pp. 297-301
    • Van Gorkom, H.J.1    Schelvis, J.P.M.2
  • 61
    • 0028908351 scopus 로고
    • Charge recombination reactions in photosystem II. 1. Yields, recombination pathways, and kinetics of the primary pair
    • F.J.E. van Mieghem, K. Brettel, B. Hillmann, A. Kamlowski, A.W. Rutherford, and E. Schlodder Charge recombination reactions in photosystem II. 1. Yields, recombination pathways, and kinetics of the primary pair Biochemistry 34 1995 4798 4813
    • (1995) Biochemistry , vol.34 , pp. 4798-4813
    • Van Mieghem, F.J.E.1    Brettel, K.2    Hillmann, B.3    Kamlowski, A.4    Rutherford, A.W.5    Schlodder, E.6
  • 62
    • 84914593918 scopus 로고
    • Kinetic and energetic model for the primary processes in photosystem II
    • G.H. Schatz, H. Brock, and A.R. Holzwarth Kinetic and energetic model for the primary processes in photosystem II Biophys. J. 54 1988 397 405
    • (1988) Biophys. J. , vol.54 , pp. 397-405
    • Schatz, G.H.1    Brock, H.2    Holzwarth, A.R.3
  • 63
    • 0032534935 scopus 로고    scopus 로고
    • Modulation of quantum yield of primary radical pair formation in photosystem II by site-directed mutagenesis affecting radical cations and anions
    • DOI 10.1021/bi980502d
    • S.A.P. Merry, P.J. Nixon, L.M.C. Barter, M.J. Schilstra, G. Porter, J. Barber, J.R. Durrant, and D. Klug Modulation of quantum yield of primary radical pair formation in photosystem II by site directed mutagenesis affecting radical cations and anions Biochemistry 37 1998 17439 17447 (Pubitemid 29013745)
    • (1998) Biochemistry , vol.37 , Issue.50 , pp. 17439-17447
    • Merry, S.A.P.1
  • 64
    • 8144219978 scopus 로고    scopus 로고
    • Modification of the pheophytin midpoint potential in Photosystem II: Modulation of the quantum yield of charge separation and of charge recombination pathways
    • A. Cuni, L. Xiong, R.T. Sayre, F. Rappaport, and J. Lavergne Modification of the pheophytin midpoint potential in Photosystem II: modulation of the quantum yield of charge separation and of charge recombination pathways Phys. Chem. Chem. Phys. 6 2004 4825 4831
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 4825-4831
    • Cuni, A.1    Xiong, L.2    Sayre, R.T.3    Rappaport, F.4    Lavergne, J.5
  • 65
    • 17144386774 scopus 로고    scopus 로고
    • Charge recombination and thermoluminescence in photosystem II
    • DOI 10.1529/biophysj.104.050237
    • F. Rappaport, A. Cuni, L. Xiong, R. Sayre, and J. Lavergne Charge recombination and thermoluminescence in photosystem II Biophys. J. 88 2005 1948 1958 (Pubitemid 40976205)
    • (2005) Biophysical Journal , vol.88 , Issue.3 , pp. 1948-1958
    • Rappaport, F.1    Cuni, A.2    Xiong, L.3    Sayre, R.4    Lavergne, J.5
  • 66
    • 0029914075 scopus 로고    scopus 로고
    • Dissipation in bioenergetic electron transfer chains
    • J. Lavergne, and P. Joliot Dissipation in bioenergetic electron transfer chains Photosynth. Res. 48 1996 127 138 (Pubitemid 26367866)
    • (1996) Photosynthesis Research , vol.48 , Issue.1-2 , pp. 127-138
    • Lavergne, J.1    Joliot, P.2
  • 67
    • 33947139255 scopus 로고    scopus 로고
    • Radiative and non-radiative charge recombination pathways in Photosystem II studied by thermoluminescence and chlorophyll fluorescence in the cyanobacterium Synechocystis 6803
    • DOI 10.1016/j.bbabio.2007.01.022, PII S0005272807000254
    • K. Cser, and I. Vass Radiative and non-radiative charge recombination pathways in Photosystem II studied by thermoluminescence and chlorophyll fluorescence in the cyanobacterium Synechocystis 6803 Biochim. Biophys. Acta 1767 2007 233 243 (Pubitemid 46400604)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.3 , pp. 233-243
    • Cser, K.1    Vass, I.2
  • 68
    • 0000746842 scopus 로고
    • The role of calcium in the pH-dependent control of photosystem-II
    • A. Krieger, and E. Weis The role of calcium in the pH-dependent control of photosystem-II Photosynth. Res. 37 1993 117 130
    • (1993) Photosynth. Res. , vol.37 , pp. 117-130
    • Krieger, A.1    Weis, E.2
  • 70
    • 0001125310 scopus 로고
    • Calcium binding to the oxygen evolving enzyme varies with the redox state of the manganese cluster
    • A.G.P. Boussac, and A.W. Rutherford Calcium binding to the oxygen evolving enzyme varies with the redox state of the manganese cluster FEBS Lett. 236 1988 432 436
    • (1988) FEBS Lett. , vol.236 , pp. 432-436
    • Boussac, A.G.P.1    Rutherford, A.W.2
  • 71
    • 70449580488 scopus 로고    scopus 로고
    • Redox potential of the primary plastoquinone electron acceptor Q(A) in photosystem II from Thermosynechococcus elongatus determined by spectroelectrochemistry
    • T. Shibamoto, Y. Kato, M. Sugiura, and T. Watanabe Redox potential of the primary plastoquinone electron acceptor Q(A) in photosystem II from Thermosynechococcus elongatus determined by spectroelectrochemistry Biochemistry 48 2009 10682 10684
    • (2009) Biochemistry , vol.48 , pp. 10682-10684
    • Shibamoto, T.1    Kato, Y.2    Sugiura, M.3    Watanabe, T.4
  • 72
    • 27144512716 scopus 로고    scopus 로고
    • Control of quinone redox potentials in Photosystem II: Electron transfer and photoprotection
    • DOI 10.1021/ja052567r
    • H. Ishikita, and E.W. Knapp Control of quinone redox potentials in photosystem II: Electron transfer and photoprotection J Am Chem Soc 127 2005 14714 14720 (Pubitemid 41511009)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.42 , pp. 14714-14720
    • Ishikita, H.1    Knapp, E.-W.2
  • 73
    • 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, and 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
  • 74
    • 0032535220 scopus 로고    scopus 로고
    • Influence of herbicide binding on the redox potential of the quinone acceptor in photosystem II: Relevance to photodamage and phytotoxicity
    • DOI 10.1021/bi9822628
    • A. Krieger-Liszkay, and A.W. Rutherford Influence of herbicide binding on the redox potential of the quinone acceptor of photosystem II: relevance to photodamage and phytotoxicity Biochemistry 37 1998 17339 17344 (Pubitemid 29013734)
    • (1998) Biochemistry , vol.37 , Issue.50 , pp. 17339-17344
    • Krieger-Liszkay, A.1    Rutherford, A.W.2
  • 75
    • 0035499362 scopus 로고    scopus 로고
    • Herbicide-induced oxidative stress in photosystem II
    • DOI 10.1016/S0968-0004(01)01953-3, PII S0968000401019533
    • A.W. Rutherford, and A. Krieger-Liszkay Herbicide-induced oxidative stress in photosystem II Trends Biochem. Sci. 26 2001 648 653 (Pubitemid 33042486)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.11 , pp. 648-653
    • Rutherford A.William1    Krieger-Liszkay, A.2
  • 76
    • 77954187664 scopus 로고    scopus 로고
    • Structures and binding sites of phenolic herbicides in the Q(B) pocket of photosystem II
    • R. Takahashi, K. Hasegawa, A. Takano, and T. Noguchi Structures and binding sites of phenolic herbicides in the Q(B) pocket of photosystem II Biochemistry 49 2010 5445 5454
    • (2010) Biochemistry , vol.49 , pp. 5445-5454
    • Takahashi, R.1    Hasegawa, K.2    Takano, A.3    Noguchi, T.4
  • 77
    • 78249233837 scopus 로고    scopus 로고
    • Probing the quinone binding site of photosystem II from Thermosynechococcus elongatus containing either PsbA1 or PsbA3 as the D1 protein through the binding characteristics of herbicides
    • A. Boussac, M. Sugiura, and F. Rappaport Probing the quinone binding site of photosystem II from Thermosynechococcus elongatus containing either PsbA1 or PsbA3 as the D1 protein through the binding characteristics of herbicides Biochim. Biophys. Acta 1807 2011 119 129
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 119-129
    • Boussac, A.1    Sugiura, M.2    Rappaport, F.3
  • 80
    • 0013685329 scopus 로고
    • Expression of a family of psbA genes encoding a photosystem II polypeptide in the cyanobacterium Anacystis nidulans R2
    • S.S. Golden, J. Brusslan, and R. Haselkorn Expression of a family of psbA genes encoding a photosystem II polypeptide in the cyanobacterium Anacystis nidulans R2 Embo J. 5 1986 2789 2798
    • (1986) Embo J. , vol.5 , pp. 2789-2798
    • Golden, S.S.1    Brusslan, J.2    Haselkorn, R.3
  • 82
    • 0034058872 scopus 로고    scopus 로고
    • Degradation of the Photosystem II D1 and D2 proteins in different strains of the cyanobacterium Synechocystis PCC 6803 varying with respect to the type and level of psbA transcript
    • DOI 10.1023/A:1006305308196
    • J. Komenda, H.A. Hassan, B.A. Diner, R.J. Debus, J. Barber, and P.J. Nixon Degradation of the Photosystem II D1 and D2 proteins in different strains of the cyanobacterium Synechocytis PCC 6803 varying with respect to the type and level of psbA transcript Plant Mol. Biol. 42 2000 635 645 (Pubitemid 30236511)
    • (2000) Plant Molecular Biology , vol.42 , Issue.4 , pp. 635-645
    • Komenda, J.1    Hassan, H.A.G.2    Diner, B.A.3    Debus, R.J.4    Barber, J.5    Nixon, P.J.6
  • 84
    • 77956899459 scopus 로고    scopus 로고
    • Functional characterization and quantification of the alternative PsbA copies in Thermosynechococcus elongatus and their role in photoprotection
    • J. Sander Functional characterization and quantification of the alternative PsbA copies in Thermosynechococcus elongatus and their role in photoprotection J. Biol. Chem. 285 2010 29851 29856
    • (2010) J. Biol. Chem. , vol.285 , pp. 29851-29856
    • Sander, J.1
  • 85
    • 77953811055 scopus 로고    scopus 로고
    • Energetics in Photosystem II from Thermosynechococcus elongatus with a D1 protein encoded by either the psbA1 or psbA3 gene
    • M. Sugiura, Y. Kato, R. Takahashi, H. Suzuki, T. Watanabe, T. Noguchi, F. Rappaport, and A. Boussac Energetics in Photosystem II from Thermosynechococcus elongatus with a D1 protein encoded by either the psbA1 or psbA3 gene Biochim. Biophys. Acta 1797 2010 1491 1499
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1491-1499
    • Sugiura, M.1    Kato, Y.2    Takahashi, R.3    Suzuki, H.4    Watanabe, T.5    Noguchi, T.6    Rappaport, F.7    Boussac, A.8
  • 86
    • 63549106377 scopus 로고    scopus 로고
    • Janus-faced charge recombinations in photosystem II photoinhibition
    • I. Vass, and K. Cser Janus-faced charge recombinations in photosystem II photoinhibition Trends Plant Sci 14 2009 200 205
    • (2009) Trends Plant Sci , vol.14 , pp. 200-205
    • Vass, I.1    Cser, K.2
  • 87
    • 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, and 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
  • 88
    • 0026696595 scopus 로고
    • Spectroscopic characterization of triplet forming states in photosystem II
    • I. Vass, and S. Styring Spectroscopic characterization of triplet forming states in photosystem II Biochemistry 31 1992 5957 5963
    • (1992) Biochemistry , vol.31 , pp. 5957-5963
    • Vass, I.1    Styring, S.2
  • 89
    • 0032551757 scopus 로고    scopus 로고
    • Reaction centre photochemistry in cyanide-treated photosystem II
    • DOI 10.1016/S0005-2728(98)00091-7, PII S0005272898000917
    • Y. Deligiannakis, and A.W. Rutherford Reaction centre photochemistry in cyanide-treated photosystem II Biochim. Biophys. Acta 1365 1998 354 362 (Pubitemid 29012393)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1365 , Issue.3 , pp. 354-362
    • Deligiannakis, Y.1    Rutherford, A.W.2
  • 91
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the Photosynthetic Oxygen-Evolving Center
    • DOI 10.1126/science.1093087
    • K.N. Ferreira, T.M. Iverson, K. Maghlaoui, J. Barber, and S. Iwata Architecture of the photosynthetic oxygen-evolving center Science 303 2004 1831 1838 (Pubitemid 38374869)
    • (2004) Science , vol.303 , Issue.5665 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 92
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial photosystem II at 2.9-A resolution and the role of quinones, lipids, channels and chloride
    • A. Guskov, J. Kern, A. Gabdulkhakov, M. Broser, A. Zouni, and W. Saenger Cyanobacterial photosystem II at 2.9-A resolution and the role of quinones, lipids, channels and chloride Nat. Struct. Mol. Biol. 16 2009 334 342
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 334-342
    • Guskov, A.1    Kern, J.2    Gabdulkhakov, A.3    Broser, M.4    Zouni, A.5    Saenger, W.6
  • 93
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 A
    • Y. Umena, K. Kawakami, J.R. Shen, and N. Kamiya Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 A 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
  • 94
    • 0025891869 scopus 로고
    • A chlorophyll tilted 30 relative to the membrane in the photosystem II reaction centre
    • F.J.E. van Mieghem, K. Satoh, and A.W. Rutherford A chlorophyll tilted 30 relative to the membrane in the photosystem II reaction centre Biochim. Biophys. Acta 1058 1991 379 385
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 379-385
    • Van Mieghem, F.J.E.1    Satoh, K.2    Rutherford, A.W.3
  • 95
    • 0035822664 scopus 로고    scopus 로고
    • Site-directed mutations at D1-His198 and D2-His197 of photosystem II in Synechocystis PCC 6803: Sites of primary charge separation and cation and triplet stabilization
    • DOI 10.1021/bi010121r
    • B.A. Diner, E. Schlodder, P.J. Nixon, W.J. Coleman, F. Rappaport, J. Lavergne, W.F. Vermaas, and D.A. Chisholm Site-directed mutations at D1-His198 and D2-His197 of photosystem II in Synechocystis PCC 6803: sites of primary charge separation and cation and triplet stabilization Biochemistry 40 2001 9265 9281 (Pubitemid 32730048)
    • (2001) Biochemistry , vol.40 , Issue.31 , pp. 9265-9281
    • Diner, B.A.1    Schlodder, E.2    Nixon, P.J.3    Coleman, W.J.4    Rappaport, F.5    Lavergne, J.6    Vermaas, W.F.J.7    Chisholm, D.A.8
  • 96
    • 0025781574 scopus 로고
    • Beta-carotene within the isolated photosystem II reaction centre: Photooxidation and irreversible bleaching of this chromophore by oxidised P680
    • A. Telfer, J.D. Rivas, and J. Barber Beta-carotene within the isolated photosystem II reaction centre: photooxidation and irreversible bleaching of this chromophore by oxidised P680 Biochim. Biophys. Acta 1060 1991 106 114
    • (1991) Biochim. Biophys. Acta , vol.1060 , pp. 106-114
    • Telfer, A.1    Rivas, J.D.2    Barber, J.3
  • 98
    • 0343618724 scopus 로고    scopus 로고
    • Dark reoxidation of the plastoquinone-pool is mediated by the low-potential form of cytochrome b-559 in spinach thylakoids
    • J. Kruk, and K. Strzalka Dark reoxidation of the plastoquinone-pool is mediated by the low-potential form of cytochrome b-559 in spinach thylakoids Photosynth. Res. 62 1999 273 279 (Pubitemid 30213282)
    • (1999) Photosynthesis Research , vol.62 , Issue.2-3 , pp. 273-279
    • Kruk, J.1    Strzalka, K.2
  • 99
    • 33846617289 scopus 로고    scopus 로고
    • Evidence for a novel quinone-binding site in the photosystem II (PS II) complex that regulates the redox potential of cytochrome b559
    • DOI 10.1021/bi0613022
    • O. Kaminskaya, V.A. Shuvalov, and G. Renger Evidence for a novel quinone-binding site in the photosystem II (PS II) complex that regulates the redox potential of cytochrome b559 Biochemistry 46 2007 1091 1105 (Pubitemid 46184996)
    • (2007) Biochemistry , vol.46 , Issue.4 , pp. 1091-1105
    • Kaminskaya, O.1    Shuvalov, V.A.2    Renger, G.3
  • 100
    • 25444441462 scopus 로고    scopus 로고
    • Secondary quinone in photosystem II of Thermosynechococcus elongatus: Semiquinone-iron EPR signals and temperature dependence of electron transfer
    • DOI 10.1021/bi051000k
    • C. Fufezan, C. Zhang, A. Krieger-Liszkay, and A.W. Rutherford Secondary quinone in photosystem II of Thermosynechococcus elongatus: semiquinone-iron EPR signals and temperature dependence of electron transfer Biochemistry 44 2005 12780 12789 (Pubitemid 41377317)
    • (2005) Biochemistry , vol.44 , Issue.38 , pp. 12780-12789
    • Fufezan, C.1    Zhang, C.2    Krieger-Liszkay, A.3    Rutherford, A.W.4
  • 101
    • 0024280216 scopus 로고
    • Cytochrome b-559 may function to protect photosystem II from photoinhibition
    • L.K. Thompson, and G.W. Brudvig Cytochrome b-559 may function to protect photosystem II from photoinhibition Biochemistry 27 1988 6653 6658
    • (1988) Biochemistry , vol.27 , pp. 6653-6658
    • Thompson, L.K.1    Brudvig, G.W.2
  • 102
    • 33746530476 scopus 로고    scopus 로고
    • Cyclic electron transfer in photosystem II in the marine diatom Phaeodactylum tricornutum
    • DOI 10.1016/j.bbabio.2006.06.003, PII S0005272806001848
    • W. Onno Feikema, M.A. Marosvolgyi, J. Lavaud, and H.J. van Gorkom Cyclic electron transfer in photosystem II in the marine diatom Phaeodactylum tricornutum Biochim. Biophys. Acta 1757 2006 829 834 (Pubitemid 44142429)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.7 , pp. 829-834
    • Onno Feikema, W.1    Marosvolgyi, M.A.2    Lavaud, J.3    Van Gorkom, H.J.4
  • 103
    • 14844362735 scopus 로고    scopus 로고
    • Redox potentials of chlorophylls in the photosystem II reaction center
    • DOI 10.1021/bi047922p
    • H. Ishikita, B. Loll, J. Biesiadka, W. Saenger, and E.W. Knapp Redox potentials of chlorophylls in the photosystem II reaction center Biochemistry 44 2005 4118 4124 (Pubitemid 40358065)
    • (2005) Biochemistry , vol.44 , Issue.10 , pp. 4118-4124
    • Ishikita, H.1    Loll, B.2    Biesiadka, J.3    Saenger, W.4    Knapp, E.-W.5
  • 104
    • 55249086054 scopus 로고    scopus 로고
    • Multiple redox-active chlorophylls in the secondary electron-transfer pathways of oxygen-evolving photosystem II
    • C.A. Tracewell, and G.W. Brudvig Multiple redox-active chlorophylls in the secondary electron-transfer pathways of oxygen-evolving photosystem II Biochemistry 47 2008 11559 11572
    • (2008) Biochemistry , vol.47 , pp. 11559-11572
    • Tracewell, C.A.1    Brudvig, G.W.2
  • 105
    • 0020173148 scopus 로고
    • A Q-cycle mechanism for the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides
    • A.R. Crofts, and S.W. Meinhardt A Q-cycle mechanism for the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides Biochem. Soc. Trans. 10 1982 193 201
    • (1982) Biochem. Soc. Trans. , vol.10 , pp. 193-201
    • Crofts, A.R.1    Meinhardt, S.W.2
  • 108
    • 0037056056 scopus 로고    scopus 로고
    • 1 complex?
    • DOI 10.1016/S0005-2728(02)00251-7, PII S0005272802002517
    • G. Brasseur, P. Bruscella, V. Bonnefoy, and D. Lemesle-Meunier The bc(1) complex of the iron-grown acidophilic chemolithotrophic bacterium Acidithiobacillus ferrooxidans functions in the reverse but not in the forward direction. Is there a second bc(1) complex? Biochim. Biophys. Acta 1555 2002 37 43 (Pubitemid 35246002)
    • (2002) Biochimica et Biophysica Acta - Bioenergetics , vol.1555 , Issue.1-3 , pp. 37-43
    • Brasseur, G.1    Bruscella, P.2    Bonnefoy, V.3    Lemesle-Meunier, D.4
  • 109
    • 79960557326 scopus 로고    scopus 로고
    • Conformationally linked interaction in the cytochrome bc(1) complex between inhibitors of the Q(o) site and the Rieske iron-sulfur protein
    • E.A. Berry, and L.S. Huang Conformationally linked interaction in the cytochrome bc(1) complex between inhibitors of the Q(o) site and the Rieske iron-sulfur protein Biochim. Biophys. Acta 1807 2011 1349 1363
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1349-1363
    • Berry, E.A.1    Huang, L.S.2
  • 110
    • 79956128428 scopus 로고    scopus 로고
    • The Q cycle of cytochrome bc complexes: A structure perspective
    • W.A. Cramer, S.S. Hasan, and 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
  • 111
    • 46449118774 scopus 로고    scopus 로고
    • The Q-cycle reviewed: How well does a monomeric mechanism of the bc(1) complex account for the function of a dimeric complex?
    • A.R. Crofts The Q-cycle reviewed: How well does a monomeric mechanism of the bc(1) complex account for the function of a dimeric complex? Biochim. Biophys. Acta 1777 2008 1001 1019
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1001-1019
    • Crofts, A.R.1
  • 112
    • 33846029501 scopus 로고    scopus 로고
    • 1 complexes of phototrophic bacteria: Introducing the activated Q-cycle
    • DOI 10.1039/b517522d
    • A.Y. Mulkidjanian Proton translocation by the cytochrome bc1 complexes of phototrophic bacteria: introducing the activated Q-cycle Photochem. Photobiol. Sci. 6 2007 19 34 (Pubitemid 46046002)
    • (2007) Photochemical and Photobiological Sciences , vol.6 , Issue.1 , pp. 19-34
    • Mulkidjanian, A.Y.1
  • 113
    • 73249144166 scopus 로고    scopus 로고
    • Visualizing changes in electron distribution in coupled chains of cytochrome bc(1) by modifying barrier for electron transfer between the FeS cluster and heme c(1)
    • E. Cieluch, K. Pietryga, M. Sarewicz, and A. Osyczka Visualizing changes in electron distribution in coupled chains of cytochrome bc(1) by modifying barrier for electron transfer between the FeS cluster and heme c(1) Biochim. Biophys. Acta 1797 2010 296 303
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 296-303
    • Cieluch, E.1    Pietryga, K.2    Sarewicz, M.3    Osyczka, A.4
  • 114
    • 1342325555 scopus 로고    scopus 로고
    • Reversible redox energy coupling in electron transfer chains
    • DOI 10.1038/nature02242
    • A. Osyczka, C.C. Moser, F. Daldal, and P.L. Dutton Reversible redox energy coupling in electron transfer chains Nature 427 2004 607 612 (Pubitemid 38248474)
    • (2004) Nature , vol.427 , Issue.6975 , pp. 607-612
    • Osyczka, A.1    Moser, C.C.2    Daldal, F.3    Dutton, P.L.4
  • 116
    • 33748913718 scopus 로고    scopus 로고
    • 1 complex: A new gating mechanism that prevents short circuits
    • DOI 10.1016/j.bbabio.2006.02.009, PII S0005272806000363
    • A.R. Crofts, S. Lhee, S.B. Crofts, J. Cheng, and S. Rose Proton pumping in the bc1 complex: a new gating mechanism that prevents short circuits Biochim. Biophys. Acta 1757 2006 1019 1034 (Pubitemid 44427755)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.8 , pp. 1019-1034
    • Crofts, A.R.1    Lhee, S.2    Crofts, S.B.3    Cheng, J.4    Rose, S.5
  • 117
    • 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, and 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
  • 118
    • 0037172774 scopus 로고    scopus 로고
    • 1 complex
    • DOI 10.1021/bi025581e
    • F. Muller, A.R. Crofts, and D.M. Kramer Multiple Q-cycle bypass reactions at the Qo site of the cytochrome bc1 complex Biochemistry 41 2002 7866 7874 (Pubitemid 34655151)
    • (2002) Biochemistry , vol.41 , Issue.25 , pp. 7866-7874
    • Muller, F.1    Crofts, A.R.2    Kramer, D.M.3
  • 120
    • 56749172576 scopus 로고    scopus 로고
    • Movement of the iron-sulfur head domain of cytochrome bc(1) transiently opens the catalytic Q(o) site for reaction with oxygen
    • A. Borek, M. Sarewicz, and A. Osyczka Movement of the iron-sulfur head domain of cytochrome bc(1) transiently opens the catalytic Q(o) site for reaction with oxygen Biochemistry 47 2008 12365 12370
    • (2008) Biochemistry , vol.47 , pp. 12365-12370
    • Borek, A.1    Sarewicz, M.2    Osyczka, A.3
  • 121
    • 77956262775 scopus 로고    scopus 로고
    • Discrimination between two possible reaction sequences that create potential risk of generation of deleterious radicals by cytochrome bc. Implications for the mechanism of superoxide production
    • M. Sarewicz, A. Borek, E. Cieluch, M. Swierczek, and A. Osyczka Discrimination between two possible reaction sequences that create potential risk of generation of deleterious radicals by cytochrome bc. Implications for the mechanism of superoxide production Biochim. Biophys. Acta 1797 2010 1820 1827
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1820-1827
    • Sarewicz, M.1    Borek, A.2    Cieluch, E.3    Swierczek, M.4    Osyczka, A.5
  • 124
    • 52049104467 scopus 로고    scopus 로고
    • The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex
    • S. Drose, and U. Brandt The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex J. Biol. Chem. 283 2008 21649 21654
    • (2008) J. Biol. Chem. , vol.283 , pp. 21649-21654
    • Drose, S.1    Brandt, U.2
  • 125
    • 67349133591 scopus 로고    scopus 로고
    • Ambivalent effects of diazoxide on mitochondrial ROS production at respiratory chain complexes i and III
    • S. Drose, P.J. Hanley, and U. Brandt Ambivalent effects of diazoxide on mitochondrial ROS production at respiratory chain complexes I and III Biochim. Biophys. Acta 1790 2009 558 565
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 558-565
    • Drose, S.1    Hanley, P.J.2    Brandt, U.3
  • 126
    • 79958275514 scopus 로고    scopus 로고
    • Highly reactive oxygen species: Detection, formation, and possible functions
    • W. Freinbichler Highly reactive oxygen species: detection, formation, and possible functions Cell Mol. Life Sci. 68 2011 2067 2079
    • (2011) Cell Mol. Life Sci. , vol.68 , pp. 2067-2079
    • Freinbichler, W.1
  • 128
    • 79952393685 scopus 로고    scopus 로고
    • Intermonomer electron transfer between the low-potential b hemes of cytochrome bc
    • P. Lanciano, D.W. Lee, H. Yang, E. Darrouzet, and F. Daldal Intermonomer electron transfer between the low-potential b hemes of cytochrome bc Biochemistry 50 2011 1651 1663
    • (2011) Biochemistry , vol.50 , pp. 1651-1663
    • Lanciano, P.1    Lee, D.W.2    Yang, H.3    Darrouzet, E.4    Daldal, F.5
  • 129
    • 34047201634 scopus 로고    scopus 로고
    • 1 complex dimer is controlled by the energized state and by impaired electron transfer between low and high potential hemes
    • DOI 10.1016/j.febslet.2007.03.037, PII S0014579307003031
    • V.P. Shinkarev, and C.A. Wraight Intermonomer electron transfer in the bc1 complex dimer is controlled by the energized state and by impaired electron transfer between low and high potential hemes FEBS Lett. 581 2007 1535 1541 (Pubitemid 46541686)
    • (2007) FEBS Letters , vol.581 , Issue.8 , pp. 1535-1541
    • Shinkarev, V.P.1    Wraight, C.A.2
  • 130
    • 49349091791 scopus 로고    scopus 로고
    • Regulatory interactions in the dimeric cytochrome bc(1) complex: The advantages of being a twin
    • R. Covian, and B.L. Trumpower Regulatory interactions in the dimeric cytochrome bc(1) complex: the advantages of being a twin Biochim. Biophys. Acta 1777 2008 1079 1091
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1079-1091
    • Covian, R.1    Trumpower, B.L.2
  • 132
    • 0344497439 scopus 로고    scopus 로고
    • 6f complex
    • DOI 10.1038/nature02155
    • D. Stroebel, Y. Choquet, J.L. Popot, and D. Picot An atypical haem in the cytochrome b(6)f complex Nature 426 2003 413 418 (Pubitemid 37490123)
    • (2003) Nature , vol.426 , Issue.6965 , pp. 413-418
    • Stroebel, D.1    Choquet, Y.2    Popot, J.-L.3    Picot, D.4
  • 133
    • 0242494128 scopus 로고    scopus 로고
    • 6f Complex of Oxygenic Photosynthesis: Tuning the Cavity
    • DOI 10.1126/science.1090165
    • G. Kurisu, H. Zhang, J.L. Smith, and W.A. Cramer Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity Science 302 2003 1009 1014 (Pubitemid 37386186)
    • (2003) Science , vol.302 , Issue.5647 , pp. 1009-1014
    • Kurisu, G.1    Zhang, H.2    Smith, J.L.3    Cramer, W.A.4
  • 136
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • C.C. Page, C.C. Moser, X. Chen, and P.L. Dutton Natural engineering principles of electron tunnelling in biological oxidation-reduction Nature 402 1999 47 52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 137
    • 33645459555 scopus 로고    scopus 로고
    • Kinetic performance and energy profile in a roller coaster electron transfer chain: A study of modified tetraheme-reaction center constructs
    • J. Alric, J. Lavergne, F. Rappaport, A. Vermeglio, K. Matsuura, K. Shimada, and K.V. Nagashima Kinetic performance and energy profile in a roller coaster electron transfer chain: a study of modified tetraheme-reaction center constructs J Am Chem Soc 128 2006 4136 4145
    • (2006) J Am Chem Soc , vol.128 , pp. 4136-4145
    • Alric, J.1    Lavergne, J.2    Rappaport, F.3    Vermeglio, A.4    Matsuura, K.5    Shimada, K.6    Nagashima, K.V.7
  • 138
    • 77749233753 scopus 로고    scopus 로고
    • Independent initiation of primary electron transfer in the two branches of the photosystem i reaction center
    • M.G. Muller, C. Slavov, R. Luthra, K.E. Redding, and A.R. Holzwarth Independent initiation of primary electron transfer in the two branches of the photosystem I reaction center Proc. Natl. Acad. Sci. USA 107 2010 4123 4128
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 4123-4128
    • Muller, M.G.1    Slavov, C.2    Luthra, R.3    Redding, K.E.4    Holzwarth, A.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.