메뉴 건너뛰기




Volumn 1817, Issue 8, 2012, Pages 1177-1190

Extended protein/water H-bond networks in photosynthetic water oxidation

Author keywords

Hydrogen bonding; Oxygen evolution; Photosynthesis; Photosystem II; Proton transfer

Indexed keywords

AMINO ACID; DICARBOXYLIC AMINO ACID; HYDROGEN; POLYELECTROLYTE; PROTON; WATER;

EID: 84862168074     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2012.03.031     Document Type: Conference Paper
Times cited : (78)

References (98)
  • 1
    • 57749104826 scopus 로고    scopus 로고
    • Photosynthetic energy conversion: Natural and artificial
    • J. Barber Photosynthetic energy conversion: natural and artificial Chem. Soc. Rev. 38 2009 185 196
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 185-196
    • Barber, J.1
  • 2
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å
    • Y. Umena, K. Kawakami, J.-R. Shen, and N. Kamiya Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å 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
  • 4
    • 82755189597 scopus 로고    scopus 로고
    • Parameterization of photosystem II photoinactivation and repair
    • D.A. Campbell, and E. Tyystjarvi Parameterization of photosystem II photoinactivation and repair Biochim. Biophys. Acta 1817 2012 258 265
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 258-265
    • Campbell, D.A.1    Tyystjarvi, E.2
  • 5
    • 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
  • 6
    • 82755193828 scopus 로고    scopus 로고
    • The roles of chloroplast proteases in the biogenesis and maintenance of photosystem II
    • W. Chi, X. Sun, and L. Zhang The roles of chloroplast proteases in the biogenesis and maintenance of photosystem II Biochim. Biophys. Acta 1817 2012 239 246
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 239-246
    • Chi, W.1    Sun, X.2    Zhang, L.3
  • 7
    • 82755197864 scopus 로고    scopus 로고
    • Structural models of the manganese complex of photosystem II and mechanistic implications
    • A. Grundmeier, and H. Dau Structural models of the manganese complex of photosystem II and mechanistic implications Biochim. Biophys. Acta 1817 2012 88 105
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 88-105
    • Grundmeier, A.1    Dau, H.2
  • 8
    • 82755161703 scopus 로고    scopus 로고
    • Structural and mechanistic investigations of photosystem II through computational methods
    • F.M. Ho Structural and mechanistic investigations of photosystem II through computational methods Biochim. Biophys. Acta 1817 2012 106 120
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 106-120
    • Ho, F.M.1
  • 9
    • 80655135259 scopus 로고    scopus 로고
    • Supramolecular organization of photosystem II in green plants
    • R. Kouril, J.P. Dekker, and E.J. Boekema Supramolecular organization of photosystem II in green plants Biochim. Biophys. Acta 1817 2012 2 12
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 2-12
    • Kouril, R.1    Dekker, J.P.2    Boekema, E.J.3
  • 10
    • 82755161715 scopus 로고    scopus 로고
    • The role of lipids in photosystem II
    • N. Mizusawa, and H. Wada The role of lipids in photosystem II Biochim. Biophys. Acta 1817 2012 194 208
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 194-208
    • Mizusawa, N.1    Wada, H.2
  • 12
    • 82755187254 scopus 로고    scopus 로고
    • Strategies for psbA gene expression in cyanobacteria, green algae and higher plants: From transcription to PSII repair
    • P. Mulo, I. Sakurai, and E.M. Aro Strategies for psbA gene expression in cyanobacteria, green algae and higher plants: from transcription to PSII repair Biochim. Biophys. Acta 1817 2012 247 257
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 247-257
    • Mulo, P.1    Sakurai, I.2    Aro, E.M.3
  • 13
    • 80053425151 scopus 로고    scopus 로고
    • Molecular mechanisms of production and scavenging of reactive oxygen species by photosystem II
    • P. Pospisil Molecular mechanisms of production and scavenging of reactive oxygen species by photosystem II Biochim. Biophys. Acta 1817 2012 218 231
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 218-231
    • Pospisil, P.1
  • 14
    • 82755197722 scopus 로고    scopus 로고
    • Photosystem II, a growing complex: Updates on newly discovered components and low molecular mass proteins
    • L.X. Shi, M. Hall, C. Funk, and W.P. Schroder Photosystem II, a growing complex: updates on newly discovered components and low molecular mass proteins Biochim. Biophys. Acta 1817 2012 13 25
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 13-25
    • Shi, L.X.1    Hall, M.2    Funk, C.3    Schroder, W.P.4
  • 15
    • 82755160818 scopus 로고    scopus 로고
    • Cytochrome b and cyclic electron transfer within photosystem II
    • K.E. Shinopoulos, and G.W. Brudvig Cytochrome b and cyclic electron transfer within photosystem II Biochim. Biophys. Acta 1817 2012 66 75
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 66-75
    • Shinopoulos, K.E.1    Brudvig, G.W.2
  • 16
    • 82755187256 scopus 로고    scopus 로고
    • Two tyrosines that changed the world: Interfacing the oxidizing power of photochemistry to water splitting in photosystem II
    • S. Styring, J. Sjöholm, and F. Mamedov Two tyrosines that changed the world: Interfacing the oxidizing power of photochemistry to water splitting in photosystem II Biochim. Biophys. Acta 1817 2012 76 87
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 76-87
    • Styring, S.1    Sjöholm, J.2    Mamedov, F.3
  • 17
    • 82755187272 scopus 로고    scopus 로고
    • Molecular mechanisms of photodamage in the Photosystem II complex
    • I. Vass Molecular mechanisms of photodamage in the Photosystem II complex Biochim. Biophys. Acta 1817 2012 209 217
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 209-217
    • Vass, I.1
  • 18
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • 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 Å resolution Nature 409 2001 739 743
    • (2001) Nature , vol.409 , 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
  • 20
    • 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
  • 21
    • 72949083473 scopus 로고    scopus 로고
    • Principles, efficiency, and blueprint character of solar-energy conversion in photosynthetic water oxidation
    • H. Dau, and I. Zaharieva Principles, efficiency, and blueprint character of solar-energy conversion in photosynthetic water oxidation Acc. Chem. Res. 42 2009 1861 1870
    • (2009) Acc. Chem. Res. , vol.42 , pp. 1861-1870
    • Dau, H.1    Zaharieva, I.2
  • 23
    • 33744992236 scopus 로고    scopus 로고
    • Reaction cycle of photosynthetic water oxidation in plants and cyanobacteria
    • response letter
    • H. Dau, and M. Haumann Reaction cycle of photosynthetic water oxidation in plants and cyanobacteria response letter Science 312 2006 1471 1472
    • (2006) Science , vol.312 , pp. 1471-1472
    • Dau, H.1    Haumann, M.2
  • 24
    • 34249860034 scopus 로고    scopus 로고
    • Photosynthetic dioxygen formation studied by time-resolved delayed fluorescence measurements - Method, rationale, and results on the activation energy of dioxygen formation
    • J. Buchta, M. Grabolle, and H. Dau Photosynthetic dioxygen formation studied by time-resolved delayed fluorescence measurements - method, rationale, and results on the activation energy of dioxygen formation Biochim. Biophys. Acta 1767 2007 565 574
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 565-574
    • Buchta, J.1    Grabolle, M.2    Dau, H.3
  • 25
    • 34547794990 scopus 로고    scopus 로고
    • Time-resolved X-ray spectroscopy leads to an extension of the classical S-state cycle model of photosynthetic oxygen evolution
    • H. Dau, and M. Haumann Time-resolved X-ray spectroscopy leads to an extension of the classical S-state cycle model of photosynthetic oxygen evolution Photosynth. Res. 92 2007 327 343
    • (2007) Photosynth. Res. , vol.92 , pp. 327-343
    • Dau, H.1    Haumann, M.2
  • 26
    • 78649504612 scopus 로고    scopus 로고
    • Water oxidation by photosystem II: H2O-D2O exchange and the influence of pH support formation of an intermediate by removal of a proton before dioxygen creation
    • L. Gerencser, and H. Dau Water oxidation by photosystem II: H2O-D2O exchange and the influence of pH support formation of an intermediate by removal of a proton before dioxygen creation Biochemistry 49 2010 10098 10106
    • (2010) Biochemistry , vol.49 , pp. 10098-10106
    • Gerencser, L.1    Dau, H.2
  • 27
    • 79953130211 scopus 로고    scopus 로고
    • Carboxylate shifts steer inter-quinone electron transfer in photosynthesis
    • P. Chernev, I. Zaharieva, H. Dau, and M. Haumann Carboxylate shifts steer inter-quinone electron transfer in photosynthesis J. Biol. Chem. 286 2011 5368 5374
    • (2011) J. Biol. Chem. , vol.286 , pp. 5368-5374
    • Chernev, P.1    Zaharieva, I.2    Dau, H.3    Haumann, M.4
  • 28
    • 79959820864 scopus 로고    scopus 로고
    • 2 + determines the entropy changes associated with the formation of transition states during water oxidation by Photosystem II
    • 2 + determines the entropy changes associated with the formation of transition states during water oxidation by Photosystem II Energy Environ. Sci. 4 2011 2520 2524
    • (2011) Energy Environ. Sci. , vol.4 , pp. 2520-2524
    • Rappaport, F.1    Ishida, N.2    Sugiura, M.3    Boussac, A.4
  • 29
    • 79955975775 scopus 로고    scopus 로고
    • Thermodynamic limitations of photosynthetic water oxidation at high proton concentrations
    • I. Zaharieva, J.M. Wichmann, and H. Dau Thermodynamic limitations of photosynthetic water oxidation at high proton concentrations J. Biol. Chem. 286 2011 18222 18228
    • (2011) J. Biol. Chem. , vol.286 , pp. 18222-18228
    • Zaharieva, I.1    Wichmann, J.M.2    Dau, H.3
  • 30
    • 34249847311 scopus 로고    scopus 로고
    • Eight steps preceding O-O bond formation in oxygenic photosynthesis - A basic reaction cycle of the photosystem II manganese complex
    • H. Dau, and M. Haumann Eight steps preceding O-O bond formation in oxygenic photosynthesis - a basic reaction cycle of the photosystem II manganese complex Biochim. Biophys. Acta 1767 2007 472 483
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 472-483
    • Dau, H.1    Haumann, M.2
  • 31
    • 38049016877 scopus 로고    scopus 로고
    • The manganese complex of photosystem II in its reaction cycle - Basic framework and possible realization at the atomic level
    • H. Dau, and M. Haumann The manganese complex of photosystem II in its reaction cycle - basic framework and possible realization at the atomic level Coord. Chem. Rev. 252 2008 273 295
    • (2008) Coord. Chem. Rev. , vol.252 , pp. 273-295
    • Dau, H.1    Haumann, M.2
  • 32
    • 57849114287 scopus 로고    scopus 로고
    • Uncovering channels in photosystem II by computer modelling: Current progress, future prospects, and lessons from analogous systems
    • F.M. Ho Uncovering channels in photosystem II by computer modelling: current progress, future prospects, and lessons from analogous systems Photosynth. Res. 98 2008 503 522
    • (2008) Photosynth. Res. , vol.98 , pp. 503-522
    • Ho, F.M.1
  • 34
    • 8144226211 scopus 로고    scopus 로고
    • 1-state: EXAFS results in relation to recent crystallographic data
    • 1-state: EXAFS results in relation to recent crystallographic data Phys. Chem. Chem. Phys. 6 2004 4781 4792
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 4781-4792
    • Dau, H.1    Liebisch, P.2    Haumann, M.3
  • 36
    • 33645219974 scopus 로고    scopus 로고
    • Rapid loss of structural motifs in the manganese complex of oxygenic photosynthesis by X-ray irradiation at 10-300 K
    • M. Grabolle, M. Haumann, C. Müller, P. Liebisch, and H. Dau Rapid loss of structural motifs in the manganese complex of oxygenic photosynthesis by X-ray irradiation at 10-300 K J. Biol. Chem. 281 2006 4580 4588
    • (2006) J. Biol. Chem. , vol.281 , pp. 4580-4588
    • Grabolle, M.1    Haumann, M.2    Müller, C.3    Liebisch, P.4    Dau, H.5
  • 38
    • 33751424725 scopus 로고    scopus 로고
    • Water-splitting chemistry of photosystem II
    • J.P. McEvoy, and G.W. Brudvig Water-splitting chemistry of photosystem II Chem. Rev. 106 2006 4455 4483
    • (2006) Chem. Rev. , vol.106 , pp. 4455-4483
    • McEvoy, J.P.1    Brudvig, G.W.2
  • 41
    • 0037271337 scopus 로고    scopus 로고
    • Balancing the central roles of the thylakoid proton gradient
    • D.M. Kramer, J.A. Cruz, and A. Kanazawa Balancing the central roles of the thylakoid proton gradient Trends Plant Sci. 8 2003 27 32
    • (2003) Trends Plant Sci. , vol.8 , pp. 27-32
    • Kramer, D.M.1    Cruz, J.A.2    Kanazawa, A.3
  • 42
    • 33646154454 scopus 로고    scopus 로고
    • A protein dynamics study of photosystem II: The effects of protein conformation on reaction center function
    • S. Vasil'ev, and D. Bruce A protein dynamics study of photosystem II: the effects of protein conformation on reaction center function Biophys. J. 90 2006 3062 3073
    • (2006) Biophys. J. , vol.90 , pp. 3062-3073
    • Vasil'Ev, S.1    Bruce, D.2
  • 43
    • 34547116864 scopus 로고    scopus 로고
    • Structural characteristics of channels and pathways in photosystem II including the identification of an oxygen channel
    • J.W. Murray, and J. Barber Structural characteristics of channels and pathways in photosystem II including the identification of an oxygen channel J. Struct. Biol. 159 2007 228 237
    • (2007) J. Struct. Biol. , vol.159 , pp. 228-237
    • Murray, J.W.1    Barber, J.2
  • 44
    • 77749255459 scopus 로고    scopus 로고
    • Tracking the flow of water through photosystem II using molecular dynamics and streamline tracing
    • S. Vassiliev, P. Comte, A. Mahboob, and D. Bruce Tracking the flow of water through photosystem II using molecular dynamics and streamline tracing Biochemistry 49 2010 1873 1881
    • (2010) Biochemistry , vol.49 , pp. 1873-1881
    • Vassiliev, S.1    Comte, P.2    Mahboob, A.3    Bruce, D.4
  • 46
    • 69849088750 scopus 로고    scopus 로고
    • Probing the accessibility of the Mn(4)Ca cluster in photosystem II: Channels calculation, noble gas derivatization, and cocrystallization with DMSO
    • A. Gabdulkhakov, A. Guskov, M. Broser, J. Kern, F. Muh, W. Saenger, and A. Zouni Probing the accessibility of the Mn(4)Ca cluster in photosystem II: channels calculation, noble gas derivatization, and cocrystallization with DMSO Structure 17 2009 1223 1234
    • (2009) Structure , vol.17 , pp. 1223-1234
    • Gabdulkhakov, A.1    Guskov, A.2    Broser, M.3    Kern, J.4    Muh, F.5    Saenger, W.6    Zouni, A.7
  • 47
    • 33744918747 scopus 로고    scopus 로고
    • Function of redox-active tyrosine in photosystem II
    • H. Ishikita, and E.W. Knapp Function of redox-active tyrosine in photosystem II Biophys. J. 90 2006 3886 3896
    • (2006) Biophys. J. , vol.90 , pp. 3886-3896
    • Ishikita, H.1    Knapp, E.W.2
  • 48
    • 38849188029 scopus 로고    scopus 로고
    • Access channels and methanol binding site to the CaMn4 cluster in Photosystem II based on solvent accessibility simulations, with implications for substrate water access
    • F.M. Ho, and S. Styring Access channels and methanol binding site to the CaMn4 cluster in Photosystem II based on solvent accessibility simulations, with implications for substrate water access Biochim. Biophys. Acta 1777 2008 140 153
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 140-153
    • Ho, F.M.1    Styring, S.2
  • 50
    • 36849039429 scopus 로고    scopus 로고
    • A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
    • K.A. Henzler-Wildman, M. Lei, V. Thai, S.J. Kerns, M. Karplus, and D. Kern A hierarchy of timescales in protein dynamics is linked to enzyme catalysis Nature 450 2007 913 916
    • (2007) Nature , vol.450 , pp. 913-916
    • Henzler-Wildman, K.A.1    Lei, M.2    Thai, V.3    Kerns, S.J.4    Karplus, M.5    Kern, D.6
  • 54
    • 0028241769 scopus 로고
    • Proton uptake by cytochrome c oxidase on reduction and on ligand binding
    • R. Mitchell, and P.R. Rich Proton uptake by cytochrome c oxidase on reduction and on ligand binding Biochim. Biophys. Acta 1186 1994 19 26
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 19-26
    • Mitchell, R.1    Rich, P.R.2
  • 56
    • 33645732495 scopus 로고    scopus 로고
    • Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase
    • I. Belevich, M.I. Verkhovsky, and M. Wikstrom 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    Wikstrom, M.3
  • 57
    • 34249787880 scopus 로고    scopus 로고
    • A cluster of carboxylic groups in PsbO protein is involved in proton transfer from the water oxidizing complex of Photosystem II
    • T. Shutova, V.V. Klimov, B. Andersson, and G. Samuelsson A cluster of carboxylic groups in PsbO protein is involved in proton transfer from the water oxidizing complex of Photosystem II Biochim. Biophys. Acta 1767 2007 434 440
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 434-440
    • Shutova, T.1    Klimov, V.V.2    Andersson, B.3    Samuelsson, G.4
  • 58
    • 72449163441 scopus 로고    scopus 로고
    • Asp157 is required for the function of PsbO, the photosystem II manganese stabilizing protein
    • H. Popelkova, A. Commet, and C.F. Yocum Asp157 is required for the function of PsbO, the photosystem II manganese stabilizing protein Biochemistry 48 2009 11920 11928
    • (2009) Biochemistry , vol.48 , pp. 11920-11928
    • Popelkova, H.1    Commet, A.2    Yocum, C.F.3
  • 59
    • 0032502005 scopus 로고    scopus 로고
    • Functional characterization of Synechocystis sp. PCC 6803 delta psbU and delta psbV mutants reveals important roles of cytochrome c-550 in cyanobacterial oxygen evolution
    • J.R. Shen, M. Qian, Y. Inoue, and R.L. Burnap Functional characterization of Synechocystis sp. PCC 6803 delta psbU and delta psbV mutants reveals important roles of cytochrome c-550 in cyanobacterial oxygen evolution Biochemistry 37 1998 1551 1558
    • (1998) Biochemistry , vol.37 , pp. 1551-1558
    • Shen, J.R.1    Qian, M.2    Inoue, Y.3    Burnap, R.L.4
  • 60
    • 0033527635 scopus 로고    scopus 로고
    • Deprotonation of the 33-kDa, extrinsic, manganese-stabilizing subunit accompanies photooxidation of manganese in photosystem II
    • R.S. Hutchison, J.J. Steenhuis, C.F. Yocum, M.R. Razeghifard, and B.A. Barry Deprotonation of the 33-kDa, extrinsic, manganese-stabilizing subunit accompanies photooxidation of manganese in photosystem II J. Biol. Chem. 274 1999 31987 31995
    • (1999) J. Biol. Chem. , vol.274 , pp. 31987-31995
    • Hutchison, R.S.1    Steenhuis, J.J.2    Yocum, C.F.3    Razeghifard, M.R.4    Barry, B.A.5
  • 61
    • 0242666399 scopus 로고    scopus 로고
    • Specific isotopic labeling and photooxidation-linked structural changes in the manganese-stabilizing subunit of photosystem II
    • R.K. Sachs, K.M. Halverson, and B.A. Barry Specific isotopic labeling and photooxidation-linked structural changes in the manganese-stabilizing subunit of photosystem II J. Biol. Chem. 278 2003 44222 44229
    • (2003) J. Biol. Chem. , vol.278 , pp. 44222-44229
    • Sachs, R.K.1    Halverson, K.M.2    Barry, B.A.3
  • 62
    • 27944453124 scopus 로고    scopus 로고
    • Structural dynamics of the manganese-stabilizing protein-effect of pH, calcium, and manganese
    • T. Shutova, J. Nikitina, G. Deikus, B. Andersson, V. Klimov, and G. Samuelsson Structural dynamics of the manganese-stabilizing protein-effect of pH, calcium, and manganese Biochemistry 44 2005 15182 15192
    • (2005) Biochemistry , vol.44 , pp. 15182-15192
    • Shutova, T.1    Nikitina, J.2    Deikus, G.3    Andersson, B.4    Klimov, V.5    Samuelsson, G.6
  • 63
    • 0032555160 scopus 로고    scopus 로고
    • The proton collecting function of the inner surface of cytochrome c oxidase from Rhodobacter sphaeroides
    • Y. Marantz, E. Nachliel, A. Aagaard, P. Brzezinski, and M. Gutman The proton collecting function of the inner surface of cytochrome c oxidase from Rhodobacter sphaeroides Proc. Natl. Acad. Sci. U. S. A. 95 1998 8590 8595
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 8590-8595
    • Marantz, Y.1    Nachliel, E.2    Aagaard, A.3    Brzezinski, P.4    Gutman, M.5
  • 65
    • 33748899467 scopus 로고    scopus 로고
    • The mechanism of proton transfer between adjacent sites on the molecular surface
    • M. Gutman, E. Nachliel, and R. Friedman The mechanism of proton transfer between adjacent sites on the molecular surface Biochim. Biophys. Acta 1757 2006 931 941
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 931-941
    • Gutman, M.1    Nachliel, E.2    Friedman, R.3
  • 66
    • 23244452408 scopus 로고    scopus 로고
    • Molecular dynamics of a protein surface: Ion-residues interactions
    • R. Friedman, E. Nachliel, and M. Gutman Molecular dynamics of a protein surface: ion-residues interactions Biophys. J. 89 2005 768 781
    • (2005) Biophys. J. , vol.89 , pp. 768-781
    • Friedman, R.1    Nachliel, E.2    Gutman, M.3
  • 67
    • 0030665489 scopus 로고    scopus 로고
    • Mechanism of proton entry into the cytoplasmic section of the proton-conducting channel of bacteriorhodopsin
    • S. Checover, E. Nachliel, N.A. Dencher, and M. Gutman Mechanism of proton entry into the cytoplasmic section of the proton-conducting channel of bacteriorhodopsin Biochemistry 36 1997 13919 13928
    • (1997) Biochemistry , vol.36 , pp. 13919-13928
    • Checover, S.1    Nachliel, E.2    Dencher, N.A.3    Gutman, M.4
  • 68
    • 80455174602 scopus 로고    scopus 로고
    • Protonation of key acidic residues is critical for the K-selectivity of the Na/K pump
    • H. Yu, I.M. Ratheal, P. Artigas, and B. Roux Protonation of key acidic residues is critical for the K-selectivity of the Na/K pump Nat. Struct. Mol. Biol. 18 2011 1159 1163
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1159-1163
    • Yu, H.1    Ratheal, I.M.2    Artigas, P.3    Roux, B.4
  • 69
    • 69249213570 scopus 로고    scopus 로고
    • Water molecules in short- and long-distance proton transfer steps of bacteriorhodopsin proton pumping
    • A.-N. Bondar, and J.C. Smith Water molecules in short- and long-distance proton transfer steps of bacteriorhodopsin proton pumping Isr. J. Chem. 49 2009 155 161
    • (2009) Isr. J. Chem. , vol.49 , pp. 155-161
    • Bondar, A.-N.1    Smith, J.C.2
  • 70
    • 80053054462 scopus 로고    scopus 로고
    • Proton storage site in bacteriorhodopsin: New insights from quantum mechanics/molecular mechanics simulations of microscopic pK(a) and infrared spectra
    • P. Goyal, N. Ghosh, P. Phatak, M. Clemens, M. Gaus, M. Elstner, and Q. Cui Proton storage site in bacteriorhodopsin: new insights from quantum mechanics/molecular mechanics simulations of microscopic pK(a) and infrared spectra J. Am. Chem. Soc. 133 2011 14981 14997
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 14981-14997
    • Goyal, P.1    Ghosh, N.2    Phatak, P.3    Clemens, M.4    Gaus, M.5    Elstner, M.6    Cui, Q.7
  • 72
    • 66249147196 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump at 2.4 A resolution
    • T. Shinoda, H. Ogawa, F. Cornelius, and C. Toyoshima Crystal structure of the sodium-potassium pump at 2.4 A resolution Nature 459 2009 446 450
    • (2009) Nature , vol.459 , pp. 446-450
    • Shinoda, T.1    Ogawa, H.2    Cornelius, F.3    Toyoshima, C.4
  • 74
    • 0028864699 scopus 로고
    • Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin
    • L.S. Brown, J. Sasaki, H. Kandori, A. Maeda, R. Needleman, and J.K. Lanyi Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin J. Biol. Chem. 270 1995 27122 27126
    • (1995) J. Biol. Chem. , vol.270 , pp. 27122-27126
    • Brown, L.S.1    Sasaki, J.2    Kandori, H.3    Maeda, A.4    Needleman, R.5    Lanyi, J.K.6
  • 75
    • 0032562215 scopus 로고    scopus 로고
    • Existence of a proton transfer chain in bacteriorhodopsin: Participation of Glu-194 in the release of protons to the extracellular surface
    • A.K. Dioumaev, H.T. Richter, L.S. Brown, M. Tanio, S. Tuzi, H. Saito, Y. Kimura, R. Needleman, and J.K. Lanyi Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface Biochemistry 37 1998 2496 2506
    • (1998) Biochemistry , vol.37 , pp. 2496-2506
    • Dioumaev, A.K.1    Richter, H.T.2    Brown, L.S.3    Tanio, M.4    Tuzi, S.5    Saito, H.6    Kimura, Y.7    Needleman, R.8    Lanyi, J.K.9
  • 76
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • L. Essen, R. Siegert, W.D. Lehmann, and D. Oesterhelt Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex Proc. Natl. Acad. Sci. U. S. A. 95 1998 11673 11678
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 11673-11678
    • Essen, L.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 77
    • 0033545872 scopus 로고    scopus 로고
    • In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy
    • C. Zscherp, J. Schlessinger, J. Tittor, D. Oesterhelt, and J. Heberle In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy Proc. Natl. Acad. Sci. U. S. A. 96 1999 5498 5503
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5498-5503
    • Zscherp, C.1    Schlessinger, J.2    Tittor, J.3    Oesterhelt, D.4    Heberle, J.5
  • 78
    • 4644318486 scopus 로고    scopus 로고
    • Assigning protonation patterns in water networks in bacteriorhodopsin based on computed IR spectra
    • R. Rousseau, V. Kleinschmidt, U.W. Schmitt, and D. Marx Assigning protonation patterns in water networks in bacteriorhodopsin based on computed IR spectra Angew. Chem. Int. Ed. Engl. 43 2004 4804 4807
    • (2004) Angew. Chem. Int. Ed. Engl. , vol.43 , pp. 4804-4807
    • Rousseau, R.1    Kleinschmidt, V.2    Schmitt, U.W.3    Marx, D.4
  • 80
    • 30144445932 scopus 로고    scopus 로고
    • Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy
    • F. Garczarek, and K. Gerwert Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy Nature 439 2006 109 112
    • (2006) Nature , vol.439 , pp. 109-112
    • Garczarek, F.1    Gerwert, K.2
  • 81
    • 0031682669 scopus 로고    scopus 로고
    • Photovoltage evidence that Glu-204 is the intermediate proton donor rather than the terminal proton release group in bacteriorhodopsin
    • I.V. Kalaidzidis, I.N. Belevich, and A.D. Kaulen Photovoltage evidence that Glu-204 is the intermediate proton donor rather than the terminal proton release group in bacteriorhodopsin FEBS Lett. 434 1998 197 200
    • (1998) FEBS Lett. , vol.434 , pp. 197-200
    • Kalaidzidis, I.V.1    Belevich, I.N.2    Kaulen, A.D.3
  • 82
    • 77955262868 scopus 로고    scopus 로고
    • Evidence from FTIR difference spectroscopy of an extensive network of hydrogen bonds near the oxygen-evolving Mn(4)Ca cluster of photosystem II involving D1-Glu65, D2-Glu312, and D1-Glu329
    • R.J. Service, W. Hillier, and R.J. Debus Evidence from FTIR difference spectroscopy of an extensive network of hydrogen bonds near the oxygen-evolving Mn(4)Ca cluster of photosystem II involving D1-Glu65, D2-Glu312, and D1-Glu329 Biochemistry 49 2010 6655 6669
    • (2010) Biochemistry , vol.49 , pp. 6655-6669
    • Service, R.J.1    Hillier, W.2    Debus, R.J.3
  • 83
    • 33646558919 scopus 로고    scopus 로고
    • Time-resolved vibrational spectroscopy detects protein-based intermediates in the photosynthetic oxygen-evolving cycle
    • B.A. Barry, I.B. Cooper, A. De Riso, S.H. Brewer, D.M. Vu, and R.B. Dyer Time-resolved vibrational spectroscopy detects protein-based intermediates in the photosynthetic oxygen-evolving cycle Proc. Natl. Acad. Sci. U.S.A. 103 2006 7288 7291
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 7288-7291
    • Barry, B.A.1    Cooper, I.B.2    De Riso, A.3    Brewer, S.H.4    Vu, D.M.5    Dyer, R.B.6
  • 84
    • 0030632978 scopus 로고    scopus 로고
    • Strong hydrogen bonds in chemistry and biology
    • C.L. Perrin, and J.B. Nielson Strong hydrogen bonds in chemistry and biology Annu. Rev. Phys. Chem. 48 1997 511 544
    • (1997) Annu. Rev. Phys. Chem. , vol.48 , pp. 511-544
    • Perrin, C.L.1    Nielson, J.B.2
  • 86
    • 0030854151 scopus 로고    scopus 로고
    • A metalloradical mechanism for the generation of oxygen from water in photosynthesis
    • C.W. Hoganson, and G.T. Babcock A metalloradical mechanism for the generation of oxygen from water in photosynthesis Science 277 1997 1953 1956
    • (1997) Science , vol.277 , pp. 1953-1956
    • Hoganson, C.W.1    Babcock, G.T.2
  • 87
    • 0002891361 scopus 로고    scopus 로고
    • Oxygen production in nature: A light-driven metalloradical enzyme process
    • C. Tommos, and G.T. Babcock Oxygen production in nature: a light-driven metalloradical enzyme process Acc. Chem. Res. 31 1998 18 25
    • (1998) Acc. Chem. Res. , vol.31 , pp. 18-25
    • Tommos, C.1    Babcock, G.T.2
  • 88
    • 41449116568 scopus 로고    scopus 로고
    • Quantum mechanics/molecular mechanics study of the catalytic cycle of water splitting in photosystem II
    • E.M. Sproviero, J.A. Gascon, J.P. McEvoy, G.W. Brudvig, and V.S. Batista Quantum mechanics/molecular mechanics study of the catalytic cycle of water splitting in photosystem II J. Am. Chem. Soc. 130 2008 3428 3442
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 3428-3442
    • Sproviero, E.M.1    Gascon, J.A.2    McEvoy, J.P.3    Brudvig, G.W.4    Batista, V.S.5
  • 89
    • 35649007241 scopus 로고    scopus 로고
    • Mutation of arginine 357 of the CP43 protein of photosystem II severely impairs the catalytic S-state cycle of the H2O oxidation complex
    • H.J. Hwang, P. Dilbeck, R.J. Debus, and R.L. Burnap Mutation of arginine 357 of the CP43 protein of photosystem II severely impairs the catalytic S-state cycle of the H2O oxidation complex Biochemistry 46 2007 11987 11997
    • (2007) Biochemistry , vol.46 , pp. 11987-11997
    • Hwang, H.J.1    Dilbeck, P.2    Debus, R.J.3    Burnap, R.L.4
  • 90
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial photosystem II at 2.9-Å 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-Å 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
  • 91
    • 0032514648 scopus 로고    scopus 로고
    • Oxygenic photosystem II: The mutation D1-D61N in Synechocystis sp. PCC 6803 retards S-state transitions without affecting electron transfer from YZ to P680 +
    • M. Hundelt, A.M. Hays, R.J. Debus, and W. Junge Oxygenic photosystem II: the mutation D1-D61N in Synechocystis sp. PCC 6803 retards S-state transitions without affecting electron transfer from YZ to P680 + Biochemistry 37 1998 14450 14456
    • (1998) Biochemistry , vol.37 , pp. 14450-14456
    • Hundelt, M.1    Hays, A.M.2    Debus, R.J.3    Junge, W.4
  • 93
    • 0036568229 scopus 로고    scopus 로고
    • Interhelical hydrogen bonds and spatial motifs in membrane proteins: Polar clamps and serine zippers
    • L. Adamian, and J. Liang Interhelical hydrogen bonds and spatial motifs in membrane proteins: polar clamps and serine zippers Proteins 47 2002 209 218
    • (2002) Proteins , vol.47 , pp. 209-218
    • Adamian, L.1    Liang, J.2
  • 94
    • 77954635029 scopus 로고    scopus 로고
    • Dynamics of SecY translocons with translocation-defective mutations
    • A.N. Bondar, C. del Val, J.A. Freites, D.J. Tobias, and S.H. White Dynamics of SecY translocons with translocation-defective mutations Structure 18 2010 847 857
    • (2010) Structure , vol.18 , pp. 847-857
    • Bondar, A.N.1    Del Val, C.2    Freites, J.A.3    Tobias, D.J.4    White, S.H.5
  • 95
    • 84857650478 scopus 로고    scopus 로고
    • Hydrogen-bond dynamics in membrane protein function
    • A.-N. Bondar, and S.H. White Hydrogen-bond dynamics in membrane protein function Biochim Biophys. Acta 1818 2012 942 950
    • (2012) Biochim Biophys. Acta , vol.1818 , pp. 942-950
    • Bondar, A.-N.1    White, S.H.2
  • 96
    • 34948875396 scopus 로고    scopus 로고
    • An activated glutamate residue identified in photosystem II at the interface between the manganese-stabilizing subunit and the D2 polypeptide
    • S. Rexroth, C.C. Wong, J.H. Park, J.R. Yates III, and B.A. Barry An activated glutamate residue identified in photosystem II at the interface between the manganese-stabilizing subunit and the D2 polypeptide J. Biol. Chem. 282 2007 27802 27809
    • (2007) J. Biol. Chem. , vol.282 , pp. 27802-27809
    • Rexroth, S.1    Wong, C.C.2    Park, J.H.3    Yates Iii, J.R.4    Barry, B.A.5
  • 97
    • 19544376279 scopus 로고    scopus 로고
    • Synthesis and assembly of thylakoid protein complexes: Multiple assembly steps of photosystem II
    • A. Rokka, M. Suorsa, A. Saleem, N. Battchikova, and E.M. Aro Synthesis and assembly of thylakoid protein complexes: multiple assembly steps of photosystem II Biochem. J. 388 2005 159 168
    • (2005) Biochem. J. , vol.388 , pp. 159-168
    • Rokka, A.1    Suorsa, M.2    Saleem, A.3    Battchikova, N.4    Aro, E.M.5
  • 98
    • 82755187237 scopus 로고    scopus 로고
    • Thylakoid protein phosphorylation in dynamic regulation of photosystem II in higher plants
    • M. Tikkanen, and E.M. Aro Thylakoid protein phosphorylation in dynamic regulation of photosystem II in higher plants Biochim. Biophys. Acta 1817 2012 232 238
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 232-238
    • Tikkanen, M.1    Aro, E.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.