메뉴 건너뛰기




Volumn 107, Issue 1, 2011, Pages 71-86

The evolution of Photosystem II: Insights into the past and future

Author keywords

Evolution; Manganese stabilizing protein; O 2 production; Photosystem II; Reaction center; Water splitting

Indexed keywords

MANGANESE; OXYGEN; WATER;

EID: 79551574173     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-010-9559-3     Document Type: Review
Times cited : (49)

References (128)
  • 1
    • 0041972320 scopus 로고
    • Laser flash-photolysis studies of electron-transfer between semi-quinone and fully reduced free flavins and horse heart cytochrome-C
    • Ahmad I, Cusanovich MA, Tollin G (1981) Laser flash-photolysis studies of electron-transfer between semi-quinone and fully reduced free flavins and horse heart cytochrome-C. Proc Natl Acad Sci USA 78:6724-6728
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6724-6728
    • Ahmad, I.1    Cusanovich, M.A.2    Tollin, G.3
  • 2
    • 13844284334 scopus 로고    scopus 로고
    • A redox switch hypothesis for the origin of two light reactions in photosynthesis
    • Allen JF (2005) A redox switch hypothesis for the origin of two light reactions in photosynthesis. FEBS Lett 579:963-968
    • (2005) FEBS Lett. , vol.579 , pp. 963-968
    • Allen, J.F.1
  • 3
    • 33846915961 scopus 로고    scopus 로고
    • Evolutionary biology-out of thin air
    • Allen JF, Martin W (2007) Evolutionary biology-out of thin air. Nature 445:610-612
    • (2007) Nature , vol.445 , pp. 610-612
    • Allen, J.F.1    Martin, W.2
  • 4
    • 79551518270 scopus 로고    scopus 로고
    • 3.45 billion year old stromatolite reef of Western Australia: A rich, large-scale record of early biota, strategies and habitats
    • Allwood A, Anderson M (2009) 3.45 billion year old stromatolite reef of Western Australia: a rich, large-scale record of early biota, strategies and habitats. Orig Life Evol Biosph 39:188-189
    • (2009) Orig. Life Evol. Biosph. , vol.39 , pp. 188-189
    • Allwood, A.1    Anderson, M.2
  • 6
    • 0035846819 scopus 로고    scopus 로고
    • Does functional photosystem II complex have an oxygen channel?
    • Anderson JM (2001) Does functional photosystem II complex have an oxygen channel? FEBS Lett 488:1-4
    • (2001) FEBS Lett. , vol.488 , pp. 1-4
    • Anderson, J.M.1
  • 7
    • 38949126973 scopus 로고    scopus 로고
    • Why did nature choose manganese to make oxygen?
    • Armstrong FA (2008) Why did nature choose manganese to make oxygen? Philos Trans R Soc B 363:1263-1270
    • (2008) Philos Trans. R Soc. B , vol.363 , pp. 1263-1270
    • Armstrong, F.A.1
  • 8
    • 0344412956 scopus 로고    scopus 로고
    • Core formation in Escherichia coli bacterioferritin requires a functional
    • Baaghil S, Lewin A, Moore GR, Le Brun NE (2003) Core formation in Escherichia coli bacterioferritin requires a functional. Biochemistry 42:14047-14056
    • (2003) Biochemistry , vol.42 , pp. 14047-14056
    • Baaghil, S.1    Lewin, A.2    Moore, G.R.3    Le Brun, N.E.4
  • 9
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock GT, Wikström M (1992) Oxygen activation and the conservation of energy in cell respiration. Nature 356:301-309
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikström, M.2
  • 10
    • 38849196324 scopus 로고    scopus 로고
    • Water as an active constituent in cell biology
    • Ball P (2008) Water as an active constituent in cell biology. Chem Rev 108:74-108
    • (2008) Chem. Rev. , vol.108 , pp. 74-108
    • Ball, P.1
  • 13
    • 8144227878 scopus 로고    scopus 로고
    • Crystal structure of cyanobacterial photosystem II at 3.2 angstrom resolution: A closer look at the Mn-cluster
    • Biesiadka J, Loll B, Kern J, Irrgang KD, Zouni A (2004) Crystal structure of cyanobacterial photosystem II at 3.2 angstrom resolution: a closer look at the Mn-cluster. Phys Chem Chem Phys 6:4733-4736
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 4733-4736
    • Biesiadka, J.1    Loll, B.2    Kern, J.3    Irrgang, K.D.4    Zouni, A.5
  • 14
    • 23744436588 scopus 로고    scopus 로고
    • The lipid A palmitoyltransferase PagP: Molecular mechanisms and role in bacterial pathogenesis
    • Bishop RE (2005) The lipid A palmitoyltransferase PagP: molecular mechanisms and role in bacterial pathogenesis. Mol Microbiol 57:900-912
    • (2005) Mol. Microbiol. , vol.57 , pp. 900-912
    • Bishop, R.E.1
  • 15
    • 67650308206 scopus 로고    scopus 로고
    • The evolution of photosynthesis and chloroplasts
    • Bjorn LO, Govindjee (2009) The evolution of photosynthesis and chloroplasts. Curr Sci 96:1466-1474
    • (2009) Curr. Sci. , vol.96 , pp. 1466-1474
    • Bjorn, L.O.1    Govindjee2
  • 16
    • 0027105895 scopus 로고
    • Origin and early evolution of photosynthesis
    • Blankenship RE (1992) Origin and early evolution of photosynthesis. Photosynth Res 33:91-111
    • (1992) Photosynth Res. , vol.33 , pp. 91-111
    • Blankenship, R.E.1
  • 18
    • 0032031956 scopus 로고    scopus 로고
    • The origin and evolution of oxygenic photosynthesis
    • Blankenship RE, Hartman H (1998) The origin and evolution of oxygenic photosynthesis. Trends Biochem Sci 23:94-97
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 94-97
    • Blankenship, R.E.1    Hartman, H.2
  • 20
    • 0023710642 scopus 로고
    • The molten globule state is involved in the translocation of proteins across membranes
    • Bychkova VE, Pain RH, Ptitsyn OB (1988) The molten globule state is involved in the translocation of proteins across membranes. FEBS Lett 238:231-234
    • (1988) FEBS Lett. , vol.238 , pp. 231-234
    • Bychkova, V.E.1    Pain, R.H.2    Ptitsyn, O.B.3
  • 21
    • 0028786047 scopus 로고
    • Evolution of energetic metabolism-the respiration-early hypothesis
    • Castresana J, Saraste M (1995) Evolution of energetic metabolism-the respiration-early hypothesis. Trends Biochem Sci 20:443-448
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 443-448
    • Castresana, J.1    Saraste, M.2
  • 22
    • 13944271319 scopus 로고    scopus 로고
    • Influence of structure on binding of chlorophylls to peptide ligands
    • Chen M, Eggink LL, Hoober JK, Larkum AWD (2005) Influence of structure on binding of chlorophylls to peptide ligands. J Am Chem Soc 127:2052-2053
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2052-2053
    • Chen, M.1    Eggink, L.L.2    Hoober, J.K.3    Larkum, A.W.D.4
  • 23
    • 57849138411 scopus 로고    scopus 로고
    • Designing photosystem II: Molecular engineering of photo-catalytic proteins
    • Conlan B (2008) Designing photosystem II: molecular engineering of photo-catalytic proteins. Photosynth Res 98:687-700
    • (2008) Photosynth Res. , vol.98 , pp. 687-700
    • Conlan, B.1
  • 25
    • 0001448365 scopus 로고
    • Synthesis and properties of Metalsubstituted myoglobins
    • Cowan JA, Gray HB (1989) Synthesis and properties of Metalsubstituted myoglobins. Inorg Chem 28:2074-2078
    • (1989) Inorg Chem. , vol.28 , pp. 2074-2078
    • Cowan, J.A.1    Gray, H.B.2
  • 26
    • 38049100652 scopus 로고    scopus 로고
    • Photoassembly of the water-oxidizing complex in photosystem II
    • Dasgupta J, Ananyev GM, Dismukes GC (2008) Photoassembly of the water-oxidizing complex in photosystem II. Coord Chem Rev 252:347-360
    • (2008) Coord Chem. Rev. , vol.252 , pp. 347-360
    • Dasgupta, J.1    Ananyev, G.M.2    Dismukes, G.C.3
  • 27
    • 34249847311 scopus 로고    scopus 로고
    • Eight steps preceding O-O bond formation in oxygenic photo synthesis-a basic reaction cycle of the photosystem II manganese complex
    • Dau H, Haumann M (2007) Eight steps preceding O-O bond formation in oxygenic photo synthesis-a basic reaction cycle of the photosystem II manganese complex. Biochim Biophys Acta Bioenerg 1767:472-483
    • (2007) Biochim. Biophys. Acta Bioenerg , vol.1767 , pp. 472-483
    • Dau, H.1    Haumann, M.2
  • 29
    • 4043080672 scopus 로고    scopus 로고
    • Analysis of the structure of the PsbO protein and its implications
    • De Las Rivas J, Barber J (2004) Analysis of the structure of the PsbO protein and its implications. Photosynth Res 81:329-343
    • (2004) Photosynth Res. , vol.81 , pp. 329-343
    • De Las Rivas, J.1    Barber, J.2
  • 30
    • 29144456629 scopus 로고    scopus 로고
    • Structure and evolution of the extrinsic proteins that stabilize the oxygen-evolving engine
    • De las Rivas J, Roman A (2005) Structure and evolution of the extrinsic proteins that stabilize the oxygen-evolving engine. Photochem Photobiol Sci 4:1003-1010
    • (2005) Photochem. Photobiol. Sci. , vol.4 , pp. 1003-1010
    • De Las Rivas, J.1    Roman, A.2
  • 33
    • 0034737598 scopus 로고    scopus 로고
    • Chlorophyll binding to peptide maquettes containing a retention motif
    • Eggink LL, Hoober JK (2000) Chlorophyll binding to peptide maquettes containing a retention motif. J Biol Chem 275:9087-9090
    • (2000) J. Biol. Chem. , vol.275 , pp. 9087-9090
    • Eggink, L.L.1    Hoober, J.K.2
  • 34
    • 0034814589 scopus 로고    scopus 로고
    • Characterization of de novo synthesized four-helix bundle proteins with Metalloporphyrin cofactors
    • Fahnenschmidt M, Bittl R, Schlodder E, Haehnel W, Lubitz W (2001) Characterization of de novo synthesized four-helix bundle proteins with Metalloporphyrin cofactors. Phys Chem Chem Phys 3:4082-4090
    • (2001) Phys. Chem. Chem. Phys. , vol.3 , pp. 4082-4090
    • Fahnenschmidt, M.1    Bittl, R.2    Schlodder, E.3    Haehnel, W.4    Lubitz, W.5
  • 35
    • 33645229307 scopus 로고    scopus 로고
    • Evolution-tracing oxygen's imprint on Earth's metabolic evolution
    • Falkowski PG (2006) Evolution-tracing oxygen's imprint on Earth's metabolic evolution. Science 311:1724-1725
    • (2006) Science , vol.311 , pp. 1724-1725
    • Falkowski, P.G.1
  • 40
    • 18644372534 scopus 로고    scopus 로고
    • Functional implications on the mechanism of the function of photosystem II including water oxidation based on the structure of photosystem II
    • Fromme P, Kern J, Loll B, Biesiadka J, Saenger W, Witt HT, Krauss N, Zouni A (2002) Functional implications on the mechanism of the function of photosystem II including water oxidation based on the structure of photosystem II. Philos Trans R Soc Lond B 357:1337-1344
    • (2002) Philos Trans. R Soc. Lond. B , vol.357 , pp. 1337-1344
    • Fromme, P.1    Kern, J.2    Loll, B.3    Biesiadka, J.4    Saenger, W.5    Witt, H.T.6    Krauss, N.7    Zouni, A.8
  • 41
    • 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
    • Gabdulkhakov A, Guskov A, Broser M, Kern J, Muh F, Saenger W, Zouni A (2009) Probing the accessibility of the Mn (4) Ca cluster in photosystem II: channels calculation, noble gas derivatization, and cocrystallization with DMSO. Structure 17:1223-1234
    • (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
  • 42
    • 0000790530 scopus 로고
    • The structure of Gloeobacter violaceus and its phycobilisomes
    • Gugliemi G, Cohen-Bazire G, Brynat DA (1981) The structure of Gloeobacter violaceus and its phycobilisomes. Arch Microbiol 129:181-189
    • (1981) Arch. Microbiol. , vol.129 , pp. 181-189
    • Gugliemi, G.1    Cohen-Bazire, G.2    Brynat, D.A.3
  • 43
    • 79551519323 scopus 로고    scopus 로고
    • Quinones, lipids, channels, and chloride ion-new insights based on the structure of Cyanobacterial 0 Photosystem 11 at 2.9 angstrom resolution
    • Guskov A, Gabdulkhakov A, Broser M, Kern J, Zouni A, Saenger W (2009a) Quinones, lipids, channels, and chloride ion-new insights based on the structure of Cyanobacterial 0 Photosystem 11 at 2.9 angstrom resolution. J Biomol Struct Dyn 26:120
    • (2009) J. Biomol. Struct. Dyn. , vol.26 , pp. 120
    • Guskov, A.1    Gabdulkhakov, A.2    Broser, M.3    Kern, J.4    Zouni, A.5    Saenger, W.6
  • 44
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial photosystem II at 2.9-angstrom resolution and the role of quinones, lipids, channels and chloride
    • Guskov A, Kern J, Gabdulkhakov A, Broser M, Zouni A, Saenger W (2009b) Cyanobacterial photosystem II at 2.9-angstrom resolution and the role of quinones, lipids, channels and chloride. Nat Struct Mol Biol 16:334-342
    • (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
  • 45
    • 0032581675 scopus 로고    scopus 로고
    • Cloning and characterization of the genes coding for two porins in the unicellular cyanobacterium Synechococcus PCC 6301
    • Hansel A, Pattus F, Jurgens UJ, Tadros MH (1998) Cloning and characterization of the genes coding for two porins in the unicellular cyanobacterium Synechococcus PCC 6301. Biochim Biophys Acta Gene Struct Expr 1399:31-39
    • (1998) Biochim. Biophys. Acta Gene Struct. Expr. , vol.1399 , pp. 31-39
    • Hansel, A.1    Pattus, F.2    Jurgens, U.J.3    Tadros, M.H.4
  • 46
    • 11844263892 scopus 로고    scopus 로고
    • 562 to an archetype cytochrome b: A mutant with bis-histidine ligation of heme iron
    • 562 to an archetype cytochrome b: a mutant with bis-histidine ligation of heme iron. Biochemistry 44:431-439
    • (2005) Biochemistry , vol.44 , pp. 431-439
    • Hay, S.1    Wydrzynski, T.2
  • 47
    • 11144242802 scopus 로고    scopus 로고
    • Protein engineering of cytochrome b (562) for quinone binding and light-induced electrons transfer
    • Hay S, Wallace BB, Smith TA, Ghiggino KP, Wydrzynski T (2004) Protein engineering of cytochrome b (562) for quinone binding and light-induced electrons transfer. Proc Natl Acad Sci USA 101:17675-17680
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17675-17680
    • Hay, S.1    Wallace, B.B.2    Smith, T.A.3    Ghiggino, K.P.4    Wydrzynski, T.5
  • 49
    • 0035861755 scopus 로고    scopus 로고
    • Substrate water exchange in photosystem II depends on the peripheral proteins
    • Hillier W, Hendry G, Burnap RL, Wydrzynski T (2001) Substrate water exchange in photosystem II depends on the peripheral proteins. J Biol Chem 276:46917-46924
    • (2001) J. Biol. Chem. , vol.276 , pp. 46917-46924
    • Hillier, W.1    Hendry, G.2    Burnap, R.L.3    Wydrzynski, T.4
  • 50
    • 70350109039 scopus 로고    scopus 로고
    • Elucidating photochemical pathways of tyrosine oxidation in an engineered bacterioferritin 'reaction centre'
    • Hingorani K, Conlan B, Hillier W, Wydrzynski T (2009) Elucidating photochemical pathways of tyrosine oxidation in an engineered bacterioferritin 'reaction centre'. Aust J Chem 62:1351-1354
    • (2009) Aust. J. Chem. , vol.62 , pp. 1351-1354
    • Hingorani, K.1    Conlan, B.2    Hillier, W.3    Wydrzynski, T.4
  • 51
    • 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
    • Ho FM, Styring S (2008) 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 Bioenerg 1777:140-153
    • (2008) Biochim. Biophys. Acta Bioenerg , vol.1777 , pp. 140-153
    • Ho, F.M.1    Styring, S.2
  • 52
    • 0033968660 scopus 로고    scopus 로고
    • Cyanobacterial cell walls: News from an unusual prokaryotic envelope
    • Hoiczyk E, Hansel A (2000) Cyanobacterial cell walls: news from an unusual prokaryotic envelope. J Bacteriol 182:1191-1199
    • (2000) J. Bacteriol. , vol.182 , pp. 1191-1199
    • Hoiczyk, E.1    Hansel, A.2
  • 54
    • 33144471312 scopus 로고    scopus 로고
    • Energetics of a possible proton exit pathway for water oxidation in photosystem II
    • Ishikita H, Saenger W, Loll B, Biesiadka J, Knapp EW (2006) Energetics of a possible proton exit pathway for water oxidation in photosystem II. Biochemistry 45:2063-2071
    • (2006) Biochemistry , vol.45 , pp. 2063-2071
    • Ishikita, H.1    Saenger, W.2    Loll, B.3    Biesiadka, J.4    Knapp, E.W.5
  • 55
    • 57849160616 scopus 로고    scopus 로고
    • Comparison of bacterial reaction centers and photosystem II
    • Kalman L, Williams JC, Allen JP (2008) Comparison of bacterial reaction centers and photosystem II. Photosynth Res 98:643-655
    • (2008) Photosynth Res. , vol.98 , pp. 643-655
    • Kalman, L.1    Williams, J.C.2    Allen, J.P.3
  • 56
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-angstrom resolution
    • Kamiya N, Shen JR (2003) Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-angstrom resolution. Proc Natl Acad Sci USA 100:98-103
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.R.2
  • 58
    • 0032502312 scopus 로고    scopus 로고
    • Reconstitution of core light-harvesting complexes of photosynthetic bacteria using chemically synthesized polypeptides. 2. Determination of structural features that stabilize complex formation and their implications for the structure of the subunit complex
    • Kehoe JW, Meadows KA, Parkes-Loach PS, Loach PA (1998) Reconstitution of core light-harvesting complexes of photosynthetic bacteria using chemically synthesized polypeptides. 2. Determination of structural features that stabilize complex formation and their implications for the structure of the subunit complex. Biochemistry 37:3418-3428
    • (1998) Biochemistry , vol.37 , pp. 3418-3428
    • Kehoe, J.W.1    Meadows, K.A.2    Parkes-Loach, P.S.3    Loach, P.A.4
  • 59
    • 0026643264 scopus 로고
    • Multiple periplasmic catalases in phytopathogenic strains of pseudomonas-syringae
    • Klotz MG, Hutcheson SW (1992) Multiple periplasmic catalases in phytopathogenic strains of pseudomonas-syringae. Appl Environ Microbiol 58:2468-2473
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2468-2473
    • Klotz, M.G.1    Hutcheson, S.W.2
  • 60
    • 0033942874 scopus 로고    scopus 로고
    • Structure and function of bacterial outer membrane proteins: Barrels in a nutshell
    • Koebnik R, Locher KP, Van Gelder P (2000) Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol Microbiol 37:239-253
    • (2000) Mol. Microbiol. , vol.37 , pp. 239-253
    • Koebnik, R.1    Locher, K.P.2    Van Gelder, P.3
  • 61
    • 46149138037 scopus 로고
    • Energetics of multielectron reactions. Photosynthetic oxygen evolution
    • Krishtalik LI (1986) Energetics of multielectron reactions. Photosynthetic oxygen evolution. Biochim Biophys Acta 849:162-171
    • (1986) Biochim. Biophys. Acta , vol.849 , pp. 162-171
    • Krishtalik, L.I.1
  • 64
    • 0035941496 scopus 로고    scopus 로고
    • Characterization of the O-2-evolving reaction catalyzed by [(terpy) (H2O) Mn-III (O) (2) Mn-IV (OH2) (terpy)] (NO3) (terpy = 2, 2′:6, 2″-terpyridine)
    • Limburg J, Vrettos JS, Chen HY, de Paula JC, Crabtree RH, Brudvig GW (2001) Characterization of the O-2-evolving reaction catalyzed by [(terpy) (H2O) Mn-III (O) (2) Mn-IV (OH2) (terpy)] (NO3) (terpy = 2, 2′:6, 2″-terpyridine). J Am Chem Soc 123:423-430
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 423-430
    • Limburg, J.1    Vrettos, J.S.2    Chen, H.Y.3    De Paula, J.C.4    Crabtree, R.H.5    Brudvig, G.W.6
  • 66
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 angstrom resolution structure of photosystem II
    • Loll B, Kern J, Saenger W, Zouni A, Biesiadka J (2005) Towards complete cofactor arrangement in the 3.0 angstrom resolution structure of photosystem II. Nature 438:1040-1044
    • (2005) Nature , vol.438 , pp. 1040-1044
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 67
    • 8144227510 scopus 로고    scopus 로고
    • Theoretical investigations of structure and mechanism of the oxygen-evolving complex in PSII
    • Lundberg M, Siegbahn PEM (2004) Theoretical investigations of structure and mechanism of the oxygen-evolving complex in PSII. Phys Chem Chem Phys 6:4772-4780
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 4772-4780
    • Lundberg, M.1    Siegbahn, P.E.M.2
  • 68
    • 0000124846 scopus 로고
    • Light, iron, Sam Granick, and the origin of life
    • Mauzerall D (1992) Light, iron, Sam Granick, and the origin of life. Photosynth Res 33:163-170
    • (1992) Photosynth Res. , vol.33 , pp. 163-170
    • Mauzerall, D.1
  • 69
    • 33751424725 scopus 로고    scopus 로고
    • Water-splitting chemistry of photosystem II
    • McEvoy JP, Brudvig GW (2006) Water-splitting chemistry of photosystem II. Chem Rev 106:4455-4483
    • (2006) Chem. Rev. , vol.106 , pp. 4455-4483
    • McEvoy, J.P.1    Brudvig, G.W.2
  • 70
    • 0032502338 scopus 로고    scopus 로고
    • Reconstitution of core light-harvesting complexes of photosynthetic bacteria using chemically synthesized polypeptides. 1. Minimal requirements for subunit formation
    • Meadows KA, Parkes-Loach PS, Kehoe JW, Loach PA (1998) Reconstitution of core light-harvesting complexes of photosynthetic bacteria using chemically synthesized polypeptides. 1. Minimal requirements for subunit formation. Biochemistry 37:3411-3417
    • (1998) Biochemistry , vol.37 , pp. 3411-3417
    • Meadows, K.A.1    Parkes-Loach, P.S.2    Kehoe, J.W.3    Loach, P.A.4
  • 71
    • 33751326986 scopus 로고    scopus 로고
    • Effects of noncovalently bound quinones on the ground and triplet states of zinc chlorins in solution and bound to de novo synthesized peptides
    • Mennenga A, Gartner W, Lubitz W, Gorner H (2006) Effects of noncovalently bound quinones on the ground and triplet states of zinc chlorins in solution and bound to de novo synthesized peptides. Phys Chem Chem Phys 8:5444-5453
    • (2006) Phys. Chem. Chem. Phys. , vol.8 , pp. 5444-5453
    • Mennenga, A.1    Gartner, W.2    Lubitz, W.3    Gorner, H.4
  • 73
    • 34547116864 scopus 로고    scopus 로고
    • Structural characteristics of channels and pathways in photosystem II including the identification of an oxygen channel
    • Murray JW, Barber J (2007) Structural characteristics of channels and pathways in photosystem II including the identification of an oxygen channel. J Struct Biol 159:228-237
    • (2007) J. Struct Biol. , vol.159 , pp. 228-237
    • Murray, J.W.1    Barber, J.2
  • 75
    • 0026538553 scopus 로고
    • Porins and specific channels of bacterial outer membranes
    • Nikaido H (1992) Porins and specific channels of bacterial outer membranes. Mol Microbiol 6:435-442
    • (1992) Mol. Microbiol. , vol.6 , pp. 435-442
    • Nikaido, H.1
  • 76
    • 33144468377 scopus 로고    scopus 로고
    • Design of a minimal polypeptide unit for bacteriochlorophyll binding and self-assembly based on photosynthetic bacterial light-harvesting proteins
    • Noy D, Dutton PL (2006) Design of a minimal polypeptide unit for bacteriochlorophyll binding and self-assembly based on photosynthetic bacterial light-harvesting proteins. Biochemistry 45:2103-2113
    • (2006) Biochemistry , vol.45 , pp. 2103-2113
    • Noy, D.1    Dutton, P.L.2
  • 77
    • 24944473851 scopus 로고    scopus 로고
    • Design of amphiphilic protein maquettes: Enhancing maquette functionality through binding of extremely hydrophobic cofactors to lipophilic domains
    • Noy D, Discher BM, Rubtsov IV, Hochstrasser RA, Dutton PL (2005) Design of amphiphilic protein maquettes: enhancing maquette functionality through binding of extremely hydrophobic cofactors to lipophilic domains. Biochemistry 44:12344-12354
    • (2005) Biochemistry , vol.44 , pp. 12344-12354
    • Noy, D.1    Discher, B.M.2    Rubtsov, I.V.3    Hochstrasser, R.A.4    Dutton, P.L.5
  • 78
    • 3042809852 scopus 로고    scopus 로고
    • Thinking about the evolution of photosynthesis
    • Olson JM, Blankenship RE (2004) Thinking about the evolution of photosynthesis. Photosynth Res 80:373-386
    • (2004) Photosynth Res. , vol.80 , pp. 373-386
    • Olson, J.M.1    Blankenship, R.E.2
  • 79
    • 38549164600 scopus 로고    scopus 로고
    • Periplasmic Cu, Zn superoxide dismutase and cytoplasmic Dps concur in protecting Salmonella enterica serovar Typhimurium from extracellular reactive oxygen species
    • Pacello F, Ceci P, Ammendola S, Pasquali P, Chiancone E, Battistoni A (2008) Periplasmic Cu, Zn superoxide dismutase and cytoplasmic Dps concur in protecting Salmonella enterica serovar Typhimurium from extracellular reactive oxygen species. Biochim Biophys Acta 1780:226-232
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 226-232
    • Pacello, F.1    Ceci, P.2    Ammendola, S.3    Pasquali, P.4    Chiancone, E.5    Battistoni, A.6
  • 80
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidationreduction
    • Page CC, Moser CC, Chen XX, Dutton PL (1999) Natural engineering principles of electron tunnelling in biological oxidationreduction. Nature 402:47-52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.X.3    Dutton, P.L.4
  • 83
    • 27544457271 scopus 로고    scopus 로고
    • Water oxidation catalyzed by a dinuclear Mn complex: A functional model for the oxygen-evolving center of photosystem II
    • Poulsen AK, Rompel A, McKenzie CJ (2005) Water oxidation catalyzed by a dinuclear Mn complex: a functional model for the oxygen-evolving center of photosystem II. Angew Chem Int Ed 44:6916-6920
    • (2005) Angew Chem. Int. Ed. , vol.44 , pp. 6916-6920
    • Poulsen, A.K.1    Rompel, A.2    McKenzie, C.J.3
  • 87
    • 1942440433 scopus 로고    scopus 로고
    • The evolutionary development of the protein complement of Photosystem 2
    • Raymond J, Blankenship RE (2004) The evolutionary development of the protein complement of Photosystem 2. Biochim Biophys Acta Bioenerg 1655:133-139
    • (2004) Biochim. Biophys. Acta Bioenerg , vol.1655 , pp. 133-139
    • Raymond, J.1    Blankenship, R.E.2
  • 88
    • 38049009377 scopus 로고    scopus 로고
    • The origin of the oxygenevolving complex
    • Raymond J, Blankenship RE (2008) The origin of the oxygenevolving complex. Coord Chem Rev 252:377-383
    • (2008) Coord Chem. Rev. , vol.252 , pp. 377-383
    • Raymond, J.1    Blankenship, R.E.2
  • 89
    • 33645211903 scopus 로고    scopus 로고
    • The effect of oxygen on biochemical networks and the evolution of complex life
    • Raymond J, Segre D (2006) The effect of oxygen on biochemical networks and the evolution of complex life. Science 311:1764-1767
    • (2006) Science , vol.311 , pp. 1764-1767
    • Raymond, J.1    Segre, D.2
  • 91
    • 0037417760 scopus 로고    scopus 로고
    • Binding of Zn-chlorin to a synthetic four-helix bundle peptide through histidine ligation
    • Razeghifard AR, Wydrzynski T (2003) Binding of Zn-chlorin to a synthetic four-helix bundle peptide through histidine ligation. Biochemistry 42:1024-1030
    • (2003) Biochemistry , vol.42 , pp. 1024-1030
    • Razeghifard, A.R.1    Wydrzynski, T.2
  • 93
    • 0742305590 scopus 로고    scopus 로고
    • Evolution of oxygenic photosynthesis: Genome-wide analysis of the OEC extrinsic proteins
    • Rivas JD, Balsera M, Barber J (2004) Evolution of oxygenic photosynthesis: genome-wide analysis of the OEC extrinsic proteins. Trends Plant Sci 9:18-25
    • (2004) Trends Plant Sci. , vol.9 , pp. 18-25
    • Rivas, J.D.1    Balsera, M.2    Barber, J.3
  • 94
    • 33749550607 scopus 로고    scopus 로고
    • Conservation of distantly related membrane proteins: Photosynthetic reaction centers share a common structural core
    • Sadekar S, Raymond J, Blankenship RE (2006) Conservation of distantly related membrane proteins: photosynthetic reaction centers share a common structural core. Mol Biol Evol 23:2001-2007
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 2001-2007
    • Sadekar, S.1    Raymond, J.2    Blankenship, R.E.3
  • 95
    • 0034788838 scopus 로고    scopus 로고
    • Water-soluble chlorophyll protein in Brassicaceae plants is a stress-induced chlorophyll-binding protein
    • Satoh H, Uchida A, Nakayama K, Okada M (2001) Water-soluble chlorophyll protein in Brassicaceae plants is a stress-induced chlorophyll-binding protein. Plant Cell Physiol 42:906-911
    • (2001) Plant Cell. Physiol. , vol.42 , pp. 906-911
    • Satoh, H.1    Uchida, A.2    Nakayama, K.3    Okada, M.4
  • 98
    • 0032169409 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of a photoactivatable flavocytochrome molecular maquette
    • Sharp RE, Moser CC, Rabanal F, Dutton PL (1998) Design, synthesis, and characterization of a photoactivatable flavocytochrome molecular maquette. Proc Natl Acad Sci USA 95:10465-10470
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10465-10470
    • Sharp, R.E.1    Moser, C.C.2    Rabanal, F.3    Dutton, P.L.4
  • 99
    • 0024408647 scopus 로고
    • Periplasmic superoxide dismutases in aquaspirillum-magnetotacticum
    • Short KA, Blakemore RP (1989) Periplasmic superoxide dismutases in aquaspirillum-magnetotacticum. Arch Microbiol 152:342-346
    • (1989) Arch. Microbiol. , vol.152 , pp. 342-346
    • Short, K.A.1    Blakemore, R.P.2
  • 100
    • 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
    • Shutovaa T, Klimov VV, Anderssona B, Samuelsson G (2007) A cluster of carboxylic groups in PsbO protein is involved in proton transfer from the water oxidizing complex of Photosystem II. Biochim Biophys Acta - Bioenergetics 1767(6):434-440
    • (2007) Biochim. Biophys. Acta - Bioenergetics , vol.1767 , Issue.6 , pp. 434-440
    • Shutovaa, T.1    Klimov, V.V.2    Anderssona, B.3    Samuelsson, G.4
  • 101
    • 47249124001 scopus 로고    scopus 로고
    • Evolutionary ecology during the rise of dioxygen in the Earth's atmosphere
    • Sleep NH, Bird DK (2008) Evolutionary ecology during the rise of dioxygen in the Earth's atmosphere. Philos Trans R Soc B 363:2651-2664
    • (2008) Philos Trans. R Soc. B , vol.363 , pp. 2651-2664
    • Sleep, N.H.1    Bird, D.K.2
  • 102
    • 33846006521 scopus 로고    scopus 로고
    • S-layers as a basic building block in a molecular construction kit
    • Sleytr UB, Egelseer EM, Ilk N, Pum D, Schuster B (2007) S-layers as a basic building block in a molecular construction kit. FEBS J 274:323-334
    • (2007) FEBS J , vol.274 , pp. 323-334
    • Sleytr, U.B.1    Egelseer, E.M.2    Ilk, N.3    Pum, D.4    Schuster, B.5
  • 104
    • 41449116568 scopus 로고    scopus 로고
    • Quantum mechanics/molecular mechanics study of the catalytic cycle of water splitting in photosystem II
    • Sproviero EM, Gascon JA, McEvoy JP, Brudvig GW, Batista VS (2008) Quantum mechanics/molecular mechanics study of the catalytic cycle of water splitting in photosystem II. J Am Chem Soc 130:3428-3442
    • (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
  • 105
    • 0000825921 scopus 로고
    • Reactions of excited-state cytochrome-C derivatives-delayed fluorescence and phosphorescence of zinc, tin, and Metal-free cytochrome-C at room-temperature
    • Sudha BP, Dixit N, Moy VT, Vanderkooi JM (1984) Reactions of excited-state cytochrome-C derivatives-delayed fluorescence and phosphorescence of zinc, tin, and Metal-free cytochrome-C at room-temperature. Biochemistry 23:2103-2107
    • (1984) Biochemistry , vol.23 , pp. 2103-2107
    • Sudha, B.P.1    Dixit, N.2    Moy, V.T.3    Vanderkooi, J.M.4
  • 106
    • 42149116995 scopus 로고    scopus 로고
    • Oxygen evolution catalysis by a dimanganese complex and its relation to photosynthetic water oxidation
    • Tagore R, Crabtree RH, Brudvig GW (2008) Oxygen evolution catalysis by a dimanganese complex and its relation to photosynthetic water oxidation. Inorg Chem 47:1815-1823
    • (2008) Inorg Chem. , vol.47 , pp. 1815-1823
    • Tagore, R.1    Crabtree, R.H.2    Brudvig, G.W.3
  • 108
    • 0002891361 scopus 로고    scopus 로고
    • Oxygen production in nature: A lightdriven Metalloradical enzyme process
    • Tommos C, Babcock GT (1998) Oxygen production in nature: a lightdriven Metalloradical enzyme process. Acc Chem Res 31:18-25
    • (1998) Acc. Chem. Res. , vol.31 , pp. 18-25
    • Tommos, C.1    Babcock, G.T.2
  • 109
    • 0034640197 scopus 로고    scopus 로고
    • Proton and hydrogen currents in photosynthetic water oxidation
    • DOI 10.1016/S0005-2728(00)00069-4, PII S0005272800000694
    • Tommos C, Babcock GT (2000) Proton and hydrogen currents in photosynthetic water oxidation. Biochim Biophys Acta Bioenerg 1458:199-219 (Pubitemid 30254260)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1458 , Issue.1 , pp. 199-219
    • Tommos, C.1    Babcock, G.T.2
  • 110
    • 0031048578 scopus 로고    scopus 로고
    • Intramolecular electron transfer kinetics of a synthetic flavocytochrome c
    • Twitchett MB, Ferrer JC, Siddarth P, Mauk AG (1997) Intramolecular electron transfer kinetics of a synthetic flavocytochrome c. J Am Chem Soc 119:435-436
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 435-436
    • Twitchett, M.B.1    Ferrer, J.C.2    Siddarth, P.3    Mauk, A.G.4
  • 111
    • 0017127249 scopus 로고
    • Metallocytochromes c: Characterization of electronic absorption and emission spectra of Sn4+ and Zn2+ cytochromes c
    • Vanderkooi JM, Adar F, Erecinska M (1976) Metallocytochromes c: characterization of electronic absorption and emission spectra of Sn4+ and Zn2+ cytochromes c. Eur J Biochem 64:381-387
    • (1976) Eur. J. Biochem. , vol.64 , pp. 381-387
    • Vanderkooi, J.M.1    Adar, F.2    Erecinska, M.3
  • 113
    • 57849159299 scopus 로고    scopus 로고
    • Structural and functional aspects of the MSP (PsbO) and study of its differences in thermophilic versus mesophilic organisms
    • Williamson AK (2008) Structural and functional aspects of the MSP (PsbO) and study of its differences in thermophilic versus mesophilic organisms. Photosynth Res 98:365-389
    • (2008) Photosynth Res. , vol.98 , pp. 365-389
    • Williamson, A.K.1
  • 114
    • 34547851703 scopus 로고    scopus 로고
    • The importance of protein-protein interactions for optimising oxygen activity in photosystem II: Reconstitution with a recombinant thioredoxin-manganese stabilising protein
    • Williamson AK, Liggins JR, Hillier W, Wydrzynski T (2007) The importance of protein-protein interactions for optimising oxygen activity in photosystem II: reconstitution with a recombinant thioredoxin-manganese stabilising protein. Photosynth Res 92:305-314
    • (2007) Photosynth Res. , vol.92 , pp. 305-314
    • Williamson, A.K.1    Liggins, J.R.2    Hillier, W.3    Wydrzynski, T.4
  • 115
    • 33745197457 scopus 로고    scopus 로고
    • Photosystem II: The water:plastoquinone oxidoreductase in photosynthesis
    • Govindjee ed, Springer, The Netherlands
    • Wydrzynski T, Satoh K (2005) Photosystem II: the water:plastoquinone oxidoreductase in photosynthesis. In: Govindjee (ed) Advances in photosynthesis and respiration, vol 25. Springer, The Netherlands
    • (2005) Advances in Photosynthesis and Respiration , vol.25
    • Wydrzynski, T.1    Satoh, K.2
  • 117
    • 0030042115 scopus 로고    scopus 로고
    • On the functional significance of substrate accessibility in the photosynthetic water oxidation mechanism
    • Wydrzynski T, Hillier W, Messinger J (1996) On the functional significance of substrate accessibility in the photosynthetic water oxidation mechanism. Physiol Plant 96:342-350
    • (1996) Physiol. Plant , vol.96 , pp. 342-350
    • Wydrzynski, T.1    Hillier, W.2    Messinger, J.3
  • 118
    • 36849037465 scopus 로고    scopus 로고
    • Engineering model proteins for Photosystem II function
    • Wydrzynski T, Hillier W, Conlan B (2007) Engineering model proteins for Photosystem II function. Photosynth Res 94:225-233
    • (2007) Photosynth Res. , vol.94 , pp. 225-233
    • Wydrzynski, T.1    Hillier, W.2    Conlan, B.3
  • 119
    • 0037001963 scopus 로고    scopus 로고
    • Complex evolution of photosynthesis
    • Xiong J, Bauer CE (2002a) Complex evolution of photosynthesis. Annu Rev Plant Biol 53:503-521
    • (2002) Annu Rev Plant Biol , vol.53 , pp. 503-521
    • Xiong, J.1    Bauer, C.E.2
  • 120
    • 0036414764 scopus 로고    scopus 로고
    • A cytochrome b origin of photosynthetic reaction centers: An evolutionary link between respiration and photosynthesis
    • Xiong J, Bauer CE (2002b) A cytochrome b origin of photosynthetic reaction centers: an evolutionary link between respiration and photosynthesis. J Mol Biol 322:1025-1037
    • (2002) J. Mol. Biol. , vol.322 , pp. 1025-1037
    • Xiong, J.1    Bauer, C.E.2
  • 121
    • 0032424309 scopus 로고    scopus 로고
    • Tracking molecular evolution of photosynthesis by characterization of a major photosynthesis gene cluster from Heliobacillus mobilis
    • Xiong J, Inoue K, Bauer CE (1998) Tracking molecular evolution of photosynthesis by characterization of a major photosynthesis gene cluster from Heliobacillus mobilis. Proc Natl Acad Sci USA 95:14851-14856
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14851-14856
    • Xiong, J.1    Inoue, K.2    Bauer, C.E.3
  • 122
    • 0040070502 scopus 로고    scopus 로고
    • Manganese cluster in photosynthesis: Where plants oxidize water to dioxygen
    • Yachandra VK, Sauer K, Klein MP (1996) Manganese cluster in photosynthesis: where plants oxidize water to dioxygen. Chem Rev 96:2927-2950
    • (1996) Chem. Rev. , vol.96 , pp. 2927-2950
    • Yachandra, V.K.1    Sauer, K.2    Klein, M.P.3
  • 123
    • 0034712683 scopus 로고    scopus 로고
    • The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin
    • Yang XO, Le Brun NE, Thomson AJ, Moore CR, Chasteen ND (2000) The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin. Biochemistry 39:4915-4923
    • (2000) Biochemistry , vol.39 , pp. 4915-4923
    • Yang, X.O.1    Le Brun, N.E.2    Thomson, A.J.3    Moore, C.R.4    Chasteen, N.D.5
  • 127
    • 0000723751 scopus 로고
    • Long-range triplet-triplet energytransfer within Metal-substituted hemoglobins
    • Zemel H, Hoffman BM (1981) Long-range triplet-triplet energytransfer within Metal-substituted hemoglobins. J Am Chem Soc 103:1192-1201
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 1192-1201
    • Zemel, H.1    Hoffman, B.M.2
  • 128
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 angstrom resolution
    • Zouni A, Witt HT, Kern J, Fromme P, Krauss N, Saenger W, Orth P (2001) Crystal structure of photosystem II from Synechococcus elongatus at 3.8 angstrom resolution. Nature 409:739-743
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.