메뉴 건너뛰기




Volumn 32, Issue , 2003, Pages 237-256

The binding of cofactors to photosystem I analyzed by spectroscopic and mutagenic methods

Author keywords

Electron paramagnetic resonance; Iron sulfur cluster; P700; Phylloquinone; X ray crystal structure

Indexed keywords

CAROTENOID; CHLOROPHYLL; COFACTOR; IRON SULFUR PROTEIN; LIGAND; PHYTOMENADIONE; POLYPEPTIDE; PROTEIN; PROTEIN P700; UNCLASSIFIED DRUG;

EID: 0012178418     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.32.110601.142356     Document Type: Review
Times cited : (42)

References (86)
  • 1
    • 0033623966 scopus 로고    scopus 로고
    • Paramagnetic 1H NMR spectroscopy of the reduced, unbound photosystem I subunit PsaC: Sequence-specific assignment of contact-shifted resonances and identification of mixed- and equal-valence Fe-Fe pairs in [4Fe-4S] centers FA- and FB-
    • Antonkine ML, Bentrop D, Bertini I, Luchinat C, Shen G, et al. 2000. Paramagnetic 1H NMR spectroscopy of the reduced, unbound photosystem I subunit PsaC: sequence-specific assignment of contact-shifted resonances and identification of mixed- and equal-valence Fe-Fe pairs in [4Fe-4S] centers FA- and FB-. J. Biol. Inorg. Chem. 5:381-92
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 381-392
    • Antonkine, M.L.1    Bentrop, D.2    Bertini, I.3    Luchinat, C.4    Shen, G.5
  • 3
    • 0015506579 scopus 로고
    • Quantitative EPR studies of the primary reaction of photosystem I in chloroplasts
    • Bearden AJ, Malkin R. 1972. Quantitative EPR studies of the primary reaction of photosystem I in chloroplasts. Biochim. Biophys. Acta 283:456-68
    • (1972) Biochim. Biophys. Acta , vol.283 , pp. 456-468
    • Bearden, A.J.1    Malkin, R.2
  • 4
    • 0030882308 scopus 로고    scopus 로고
    • Pulsed EPR structure analysis of photosystem I single crystals: Localization of the phylloquinone acceptor
    • Bittl R, Zech SG, Fromme P, Witt HT, Lubitz W. 1997. Pulsed EPR structure analysis of photosystem I single crystals: localization of the phylloquinone acceptor. Biochemistry 36:12001-4
    • (1997) Biochemistry , vol.36 , pp. 12001-12004
    • Bittl, R.1    Zech, S.G.2    Fromme, P.3    Witt, H.T.4    Lubitz, W.5
  • 5
    • 0000828936 scopus 로고
    • Identification of multiple components in the intermediary electron carrier complex of photosystem I
    • Bonnerjea J, Evans MCW. 1982. Identification of multiple components in the intermediary electron carrier complex of photosystem I. FEBS Lett. 148:313-16
    • (1982) FEBS Lett. , vol.148 , pp. 313-316
    • Bonnerjea, J.1    Evans, M.C.W.2
  • 6
    • 0023656086 scopus 로고
    • Identification of a chloroplast-encoded 9-kDa polypeptide as a 2[4Fe-4S] protein carrying centers A and B of photosystem I
    • Bordier Høj P, Svendsen I, Vibe Scheller H, Lindberg Møller B. 1987. Identification of a chloroplast-encoded 9-kDa polypeptide as a 2[4Fe-4S] protein carrying centers A and B of photosystem I. J. Biol. Chem. 262:12676-84
    • (1987) J. Biol. Chem. , vol.262 , pp. 12676-12684
    • Bordier Høj, P.1    Svendsen, I.2    Vibe Scheller, H.3    Lindberg Møller, B.4
  • 7
    • 0035813110 scopus 로고    scopus 로고
    • Mutations in both sides of the photosystem I reaction center identify the phylloquinone observed by electron paramagnetic resonance spectroscopy
    • Boudreaux B, MacMillan F, Teutloff C, Agalarov R, Gu F, et al. 2001. Mutations in both sides of the photosystem I reaction center identify the phylloquinone observed by electron paramagnetic resonance spectroscopy. J. Biol. Chem. 276:37299-306
    • (2001) J. Biol. Chem. , vol.276 , pp. 37299-37306
    • Boudreaux, B.1    MacMillan, F.2    Teutloff, C.3    Agalarov, R.4    Gu, F.5
  • 8
    • 0035976011 scopus 로고    scopus 로고
    • Electron transfer in photosystem I
    • Brettel K, Leibl W. 2001. Electron transfer in photosystem I. Biochim. Biophys. Acta 1507:100-14
    • (2001) Biochim. Biophys. Acta , vol.1507 , pp. 100-114
    • Brettel, K.1    Leibl, W.2
  • 9
    • 0016701557 scopus 로고
    • EPR spectra of iron-sulfur proteins in dimethyl sulfoxide solutions. Evidence that chloroplast photosystem I particles contain 4Fe-4S centers
    • Cammack R, Evans MCW. 1975. EPR spectra of iron-sulfur proteins in dimethyl sulfoxide solutions. Evidence that chloroplast photosystem I particles contain 4Fe-4S centers. Biochem. Biophys. Res. Commun. 67:544-49
    • (1975) Biochem. Biophys. Res. Commun. , vol.67 , pp. 544-549
    • Cammack, R.1    Evans, M.C.W.2
  • 10
    • 0002662427 scopus 로고
    • Direct determination of the midpoint potential of the acceptor X in chloroplast photosystem I by electrochemical reduction and ESR spectroscopy
    • Chamorovsky SK, Cammack R. 1982. Direct determination of the midpoint potential of the acceptor X in chloroplast photosystem I by electrochemical reduction and ESR spectroscopy. Photobiochem. Photobiophys. 4:195-200
    • (1982) Photobiochem. Photobiophys. , vol.4 , pp. 195-200
    • Chamorovsky, S.K.1    Cammack, R.2
  • 11
    • 0025323166 scopus 로고
    • Spectroscopic characterization of the novel iron-sulfur cluster in Pyrococcus furiosus ferredoxin
    • Conover RC, Kowal AT, Fu WG, Park JB, Aono S, et al. 1990. Spectroscopic characterization of the novel iron-sulfur cluster in Pyrococcus furiosus ferredoxin. J. Biol. Chem. 265:8533-41
    • (1990) J. Biol. Chem. , vol.265 , pp. 8533-8541
    • Conover, R.C.1    Kowal, A.T.2    Fu, W.G.3    Park, J.B.4    Aono, S.5
  • 12
    • 0027208089 scopus 로고
    • Modulation analysis of the electron spin echo signals of in vivo oxidised primary donor N-14 chlorophyll centres in bacterial, P870 and P960, and plant photosystem-I, P700, reaction centres
    • Davis IH, Heathcote P, Maclachlan DJ, Evans MCW. 1993. Modulation analysis of the electron spin echo signals of in vivo oxidised primary donor N-14 chlorophyll centres in bacterial, P870 and P960, and plant photosystem-I, P700, reaction centres. Biochim. Biophys. Acta 1143:183-89
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 183-189
    • Davis, I.H.1    Heathcote, P.2    Maclachlan, D.J.3    Evans, M.C.W.4
  • 13
    • 0002929188 scopus 로고
    • Localization and nucleotide sequence of the gene for the 8 kDa subunit of photosystem I in pea and wheat chloroplast DNA
    • Dunn PPJ, Gray JC. 1988. Localization and nucleotide sequence of the gene for the 8 kDa subunit of photosystem I in pea and wheat chloroplast DNA. Plant Mol. Biol. 11:311-19
    • (1988) Plant Mol. Biol. , vol.11 , pp. 311-319
    • Dunn, P.P.J.1    Gray, J.C.2
  • 14
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: Cofactors and protein-cofactor interactions
    • Ermler U, Fritzsch G, Buchanan SK, Michel H. 1994. Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: cofactors and protein-cofactor interactions. Structure 2:925-36
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 15
    • 0019600926 scopus 로고
    • Mössbauer spectroscopic studies of the nature of center X of photosystem I reaction centers from the cyanobacterium Chlorogloea fritschii
    • Evans EH, Dickson DPE, Johnson CE, Rush JD, Evans MCW. 1981. Mössbauer spectroscopic studies of the nature of center X of photosystem I reaction centers from the cyanobacterium Chlorogloea fritschii. Eur. J. Biochem. 118:81-84
    • (1981) Eur. J. Biochem. , vol.118 , pp. 81-84
    • Evans, E.H.1    Dickson, D.P.E.2    Johnson, C.E.3    Rush, J.D.4    Evans, M.C.W.5
  • 16
    • 0017083870 scopus 로고
    • The properties of the primary electron acceptor in the photosystem I reaction center of spinach chloroplasts and its interaction with P700 and the bound ferredoxin in various oxidation-reduction states
    • Evans MCW, Sihra CK, Cammack R. 1976. The properties of the primary electron acceptor in the photosystem I reaction center of spinach chloroplasts and its interaction with P700 and the bound ferredoxin in various oxidation-reduction states. Biochem. J. 158:71-77
    • (1976) Biochem. J. , vol.158 , pp. 71-77
    • Evans, M.C.W.1    Sihra, C.K.2    Cammack, R.3
  • 17
    • 0015520706 scopus 로고
    • Evidence for the role of a bound ferredoxin as the primary electron acceptor of photosystem I in spinach chloroplasts
    • Evans MCW, Telfer A, Lord AV. 1972. Evidence for the role of a bound ferredoxin as the primary electron acceptor of photosystem I in spinach chloroplasts. Biochim. Biophys. Acta 267:530-37
    • (1972) Biochim. Biophys. Acta , vol.267 , pp. 530-537
    • Evans, M.C.W.1    Telfer, A.2    Lord, A.V.3
  • 19
    • 0342618603 scopus 로고    scopus 로고
    • Targeted mutations in the psaC gene of Chlamydomonas reinhardtii: Preferential reduction of F-B at low temperature is not accompanied by altered electron flow from photosystem I ferredoxin
    • Fischer N, Sétif P, Rochaix JD. 1997. Targeted mutations in the psaC gene of Chlamydomonas reinhardtii: Preferential reduction of F-B at low temperature is not accompanied by altered electron flow from photosystem I ferredoxin. Biochemistry 36:93-102
    • (1997) Biochemistry , vol.36 , pp. 93-102
    • Fischer, N.1    Sétif, P.2    Rochaix, J.D.3
  • 20
    • 0022422503 scopus 로고
    • Two partially homologous adjacent light-inducible maize chloroplast genes encoding polypeptides of the P700 chlorophyll a-protein complex of photosystem I
    • Fish LE, Kuck U, Bogorad L. 1985. Two partially homologous adjacent light-inducible maize chloroplast genes encoding polypeptides of the P700 chlorophyll a-protein complex of photosystem I. J. Biol. Chem. 260:1413-21
    • (1985) J. Biol. Chem. , vol.260 , pp. 1413-1421
    • Fish, L.E.1    Kuck, U.2    Bogorad, L.3
  • 21
    • 0023557591 scopus 로고
    • Structure, function and organization of the photosystem I reaction center complex
    • Golbeck JH. 1987. Structure, function and organization of the photosystem I reaction center complex. Biochim. Biophys. Acta 895:167-204
    • (1987) Biochim. Biophys. Acta , vol.895 , pp. 167-204
    • Golbeck, J.H.1
  • 22
    • 0032696532 scopus 로고    scopus 로고
    • B → ferredoxin/flavodoxin
    • B → ferredoxin/flavodoxin. Photosyn. Res. 61:107-49
    • (1999) Photosyn. Res. , vol.61 , pp. 107-149
    • Golbeck, J.H.1
  • 24
    • 0018790149 scopus 로고
    • Redox titration of electron acceptor Q and the plastoquinone pool in photosystem II
    • Golbeck JH, Kok B. 1979. Redox titration of electron acceptor Q and the plastoquinone pool in photosystem II. Biochim. Biophys. Acta 547:347-60
    • (1979) Biochim. Biophys. Acta , vol.547 , pp. 347-360
    • Golbeck, J.H.1    Kok, B.2
  • 27
    • 0000731555 scopus 로고
    • Analysis of the proposed Fe-Sx binding region of photosystem I by site-directed mutation of PsaA in Chlamydomonas reinhardtii
    • Hallahan BJ, Purton S, Ivison A, Wright D, Evans MCW. 1995. Analysis of the proposed Fe-Sx binding region of photosystem I by site-directed mutation of PsaA in Chlamydomonas reinhardtii. Photosynth. Res. 46:257-64
    • (1995) Photosynth. Res. , vol.46 , pp. 257-264
    • Hallahan, B.J.1    Purton, S.2    Ivison, A.3    Wright, D.4    Evans, M.C.W.5
  • 29
    • 0023476443 scopus 로고
    • The gene for the 9 kd polypeptide, a possible apoprotein for the iron-sulfur centers A and B of the photosystem I complex, in tobacco chloroplast DNA
    • Hayashida N, Matsubayashi T, Shinozaki K, Sugiura M, Inoue K, Hiyama T. 1987. The gene for the 9 kd polypeptide, a possible apoprotein for the iron-sulfur centers A and B of the photosystem I complex, in tobacco chloroplast DNA. Curr. Genet. 12:247-50
    • (1987) Curr. Genet. , vol.12 , pp. 247-250
    • Hayashida, N.1    Matsubayashi, T.2    Shinozaki, K.3    Sugiura, M.4    Inoue, K.5    Hiyama, T.6
  • 30
    • 0023057047 scopus 로고
    • The 110-kDa reaction center protein of photosystem I, P700-chlorophyll a-protein 1, is an iron-sulfur protein
    • Høj PB, Møller BL. 1986. The 110-kDa reaction center protein of photosystem I, P700-chlorophyll a-protein 1, is an iron-sulfur protein. J. Biol. Chem. 261:14292-300
    • (1986) J. Biol. Chem. , vol.261 , pp. 14292-14300
    • Høj, P.B.1    Møller, B.L.2
  • 31
    • 0035976001 scopus 로고    scopus 로고
    • Modification of photosystem I reaction center by the extraction and exchange of chlorophylls and quinones
    • Itoh S, Iwaki M, Ikegami I. 2001. Modification of photosystem I reaction center by the extraction and exchange of chlorophylls and quinones. Biochim. Biophys. Acta 1507:115-38
    • (2001) Biochim. Biophys. Acta , vol.1507 , pp. 115-138
    • Itoh, S.1    Iwaki, M.2    Ikegami, I.3
  • 32
    • 0034708819 scopus 로고    scopus 로고
    • 1 site of photosystem I. I. Genetic and physiological characterization of phylloquinone biosynthetic pathway mutants in Synechocystis sp. PCC 6803
    • 1 site of photosystem I. I. Genetic and physiological characterization of phylloquinone biosynthetic pathway mutants in Synechocystis sp. PCC 6803. J. Biol. Chem. 275:8523-30
    • (2000) J. Biol. Chem. , vol.275 , pp. 8523-8530
    • Johnson, T.W.1    Shen, G.2    Zybailov, B.3    Kolling, D.4    Reategui, R.5
  • 33
    • 0035955726 scopus 로고    scopus 로고
    • 1 site of photosystem I. In vivo replacement of plastoquinone-9 by media-supplemented naphthoquinones in phylloquinone biosynthetic pathway mutants of Synechocystis sp. PCC 6803
    • 1 site of photosystem I. In vivo replacement of plastoquinone-9 by media-supplemented naphthoquinones in phylloquinone biosynthetic pathway mutants of Synechocystis sp. PCC 6803. J. Biol. Chem. 276:39512-21
    • (2001) J. Biol. Chem. , vol.276 , pp. 39512-39521
    • Johnson, T.W.1    Zybailov, B.2    Jones, A.D.3    Bittl, R.4    Zech, S.5
  • 36
    • 0037022784 scopus 로고    scopus 로고
    • The function of photosystem I. Quantum chemical insight into the role of tryptophan-quinone interactions
    • Kaupp M. 2002. The function of photosystem I. Quantum chemical insight into the role of tryptophan-quinone interactions. Biochemistry 41:2895-900
    • (2002) Biochemistry , vol.41 , pp. 2895-2900
    • Kaupp, M.1
  • 37
    • 0033548585 scopus 로고    scopus 로고
    • Photosystem I, an improved model of the stromal subunits PsaC, PsaD, and PsaE
    • Klukas O, Schubert WD, Jordan P, Krauß N, Fromme P, et al. 1999. Photosystem I, an improved model of the stromal subunits PsaC, PsaD, and PsaE. J. Biol. Chem. 274:7351-60
    • (1999) J. Biol. Chem. , vol.274 , pp. 7351-7360
    • Klukas, O.1    Schubert, W.D.2    Jordan, P.3    Krauß, N.4    Fromme, P.5
  • 38
    • 0034711090 scopus 로고    scopus 로고
    • Influence of the axial ligands on the spectral properties of P700 of photosystem I: A study of site-directed mutants
    • Krabben L, Schlodder E, Jordan R, Carbonera D, Giacometti G, et al. 2000. Influence of the axial ligands on the spectral properties of P700 of photosystem I: a study of site-directed mutants. Biochemistry 39:13012-25
    • (2000) Biochemistry , vol.39 , pp. 13012-13025
    • Krabben, L.1    Schlodder, E.2    Jordan, R.3    Carbonera, D.4    Giacometti, G.5
  • 39
    • 0027535808 scopus 로고
    • 3-Dimensional structure of system-I of photosynthesis at 6 Å resolution
    • Krauß N, Hinrichs W, Witt I, Fromme P, Pritzkow W, et al. 1993. 3-Dimensional structure of system-I of photosynthesis at 6 Å resolution. Nature 361:326-31
    • (1993) Nature , vol.361 , pp. 326-331
    • Krauß, N.1    Hinrichs, W.2    Witt, I.3    Fromme, P.4    Pritzkow, W.5
  • 40
    • 0029911269 scopus 로고    scopus 로고
    • Photosystem I at 4 Å resolution represents the first structural model of a joint photosynthetic reaction centre and core antenna system
    • Krauß N, Schubert WD, Klukas O, Fromme P, Witt HT, Saenger W. 1996. Photosystem I at 4 Å resolution represents the first structural model of a joint photosynthetic reaction centre and core antenna system. Nat. Struct. Biol. 3:965-73
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 965-973
    • Krauß, N.1    Schubert, W.D.2    Klukas, O.3    Fromme, P.4    Witt, H.T.5    Saenger, W.6
  • 43
  • 44
    • 0028042404 scopus 로고
    • The PsaC protein is necessary for the stable association of the PsaD, PsaE, and PsaL proteins in the photosystem I complex: Analysis of a cyanobacterial mutant strain
    • Mannan RM, Pakrasi HB, Sonoike K. 1994. The PsaC protein is necessary for the stable association of the PsaD, PsaE, and PsaL proteins in the photosystem I complex: analysis of a cyanobacterial mutant strain. Arch. Biochem. Biophys. 315:68-73
    • (1994) Arch. Biochem. Biophys. , vol.315 , pp. 68-73
    • Mannan, R.M.1    Pakrasi, H.B.2    Sonoike, K.3
  • 48
    • 0015024854 scopus 로고
    • Electron spin resonance of chlorophyll and the origin of signal I in photosynthesis
    • Norris RJ, Uphaus RA, Crespi HL, Katz JJ. 1971. Electron spin resonance of chlorophyll and the origin of signal I in photosynthesis. Proc. Natl. Acad. Sci. USA 68:625-28
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 625-628
    • Norris, R.J.1    Uphaus, R.A.2    Crespi, H.L.3    Katz, J.J.4
  • 50
    • 0035916248 scopus 로고    scopus 로고
    • Site-directed mutagenesis of PsaA residue W693 affects phylloquinone binding and function in the photosystem I reaction center of Chlamydomonas reinhardtii
    • Purton S, Stevens DR, Muhiuddin IP, Evans MC, Carter S, et al. 2001. Site-directed mutagenesis of PsaA residue W693 affects phylloquinone binding and function in the photosystem I reaction center of Chlamydomonas reinhardtii. Biochemistry 40:2167-75
    • (2001) Biochemistry , vol.40 , pp. 2167-2175
    • Purton, S.1    Stevens, D.R.2    Muhiuddin, I.P.3    Evans, M.C.4    Carter, S.5
  • 52
    • 0029012645 scopus 로고
    • ENDOR studies of the primary donor cation radical in mutant reaction centers of Rhodobacter sphaeroides with altered hydrogen-bond interactions
    • Rautter J, Lendzian F, Schulz C, Fetsch A, Kuhn M, et al. 1995. ENDOR studies of the primary donor cation radical in mutant reaction centers of Rhodobacter sphaeroides with altered hydrogen-bond interactions. Biochemistry 34:8130-43
    • (1995) Biochemistry , vol.34 , pp. 8130-8143
    • Rautter, J.1    Lendzian, F.2    Schulz, C.3    Fetsch, A.4    Kuhn, M.5
  • 53
    • 0032472375 scopus 로고    scopus 로고
    • A systematic survey of conserved histidines in the core subunits of photosystem I by site-directed mutagenesis reveals the likely axial ligands of P700
    • Redding K, MacMillan F, Leibl W, Brettel K, Hanley J, et al. 1998. A systematic survey of conserved histidines in the core subunits of photosystem I by site-directed mutagenesis reveals the likely axial ligands of P700. EMBO J. 17:50-60
    • (1998) EMBO J. , vol.17 , pp. 50-60
    • Redding, K.1    MacMillan, F.2    Leibl, W.3    Brettel, K.4    Hanley, J.5
  • 55
    • 0029834642 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the subunit PsaC establishes a surface-exposed domain interacting with the photosystem I core binding site
    • Rodday SM, Do LT, Chynwat V, Frank HA, Biggins J. 1996. Site-directed mutagenesis of the subunit PsaC establishes a surface-exposed domain interacting with the photosystem I core binding site. Biochemistry 35:11832-38
    • (1996) Biochemistry , vol.35 , pp. 11832-11838
    • Rodday, S.M.1    Do, L.T.2    Chynwat, V.3    Frank, H.A.4    Biggins, J.5
  • 57
    • 0028321236 scopus 로고
    • Structure-function studies on the interaction of PsaC with the photosystem 1 heterodimer. The site directed change R561E in PsaB destabilizes the subunit interaction in Synechocystis sp. PCC 6803
    • Rodday SM, Schulz R, McIntosh L, Biggins J. 1994. Structure-function studies on the interaction of PsaC with the photosystem 1 heterodimer. The site directed change R561E in PsaB destabilizes the subunit interaction in Synechocystis sp. PCC 6803. Photosynth. Res. 42:185-90
    • (1994) Photosynth. Res. , vol.42 , pp. 185-190
    • Rodday, S.M.1    Schulz, R.2    McIntosh, L.3    Biggins, J.4
  • 58
    • 0028988965 scopus 로고
    • X domain in photosystem I interacts with the subunit PsaC: Site-directed changes in PsaB destabilize the subunit interaction in Chlamydomonas reinhardtii
    • X domain in photosystem I interacts with the subunit PsaC: Site-directed changes in PsaB destabilize the subunit interaction in Chlamydomonas reinhardtii. Biochemistry 34:6328-34
    • (1995) Biochemistry , vol.34 , pp. 6328-6334
    • Rodday, S.M.1    Webber, A.N.2    Bingham, S.E.3    Biggins, J.4
  • 60
    • 34249929498 scopus 로고
    • Effects of selective destruction of iron-sulfur center B on electron transfer and charge recombination in photosystem I
    • Sakurai H, Inoue K, Fujii T, Mathis P. 1991. Effects of selective destruction of iron-sulfur center B on electron transfer and charge recombination in photosystem I. Photosynth. Res. 27:65-71
    • (1991) Photosynth. Res. , vol.27 , pp. 65-71
    • Sakurai, H.1    Inoue, K.2    Fujii, T.3    Mathis, P.4
  • 61
    • 0031563799 scopus 로고    scopus 로고
    • Photosystem I of Synechococcus elongatus at 4 Å resolution: Comprehensive structure analysis
    • Schubert WD, Klukas O, Krauss N, Saenger W, Fromme P, Witt HT. 1997. Photosystem I of Synechococcus elongatus at 4 Å resolution: comprehensive structure analysis. J. Mol. Biol. 272:741-69
    • (1997) J. Mol. Biol. , vol.272 , pp. 741-769
    • Schubert, W.D.1    Klukas, O.2    Krauss, N.3    Saenger, W.4    Fromme, P.5    Witt, H.T.6
  • 62
    • 0034604291 scopus 로고    scopus 로고
    • 1 site of photosystem I. Altered kinetics of electron transfer in phylloquinone biosynthetic pathway mutants studied by time-resolved optical, EPR, and electrometric techniques
    • 1 site of photosystem I. Altered kinetics of electron transfer in phylloquinone biosynthetic pathway mutants studied by time-resolved optical, EPR, and electrometric techniques. J. Biol. Chem. 275:23429-38
    • (2000) J. Biol. Chem. , vol.275 , pp. 23429-23438
    • Semenov, A.Y.1    Vassiliev, I.R.2    Van Der Est, A.3    Mamedov, M.D.4    Zybailov, B.5
  • 64
    • 0027497430 scopus 로고
    • Mutational analysis of the structure and biogenesis of the photosystem-I reaction center in the cyanobacterium Synechocystis sp. PCC 6803
    • Smart LB, Warren PV, Golbeck JH, McIntosh L. 1993. Mutational analysis of the structure and biogenesis of the photosystem-I reaction center in the cyanobacterium Synechocystis sp. PCC 6803. Proc. Natl. Acad. Sci. USA 90:1132-36
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1132-1136
    • Smart, L.B.1    Warren, P.V.2    Golbeck, J.H.3    McIntosh, L.4
  • 66
    • 0001411126 scopus 로고
    • Anisotropic electron spin polarization of correlated spin pairs in photosynthetic reaction centers
    • Stehlik D, Bock CH, Petersen J. 1989. Anisotropic electron spin polarization of correlated spin pairs in photosynthetic reaction centers. J. Phys. Chem. 93:1612-19
    • (1989) J. Phys. Chem. , vol.93 , pp. 1612-1619
    • Stehlik, D.1    Bock, C.H.2    Petersen, J.3
  • 67
    • 0001738702 scopus 로고
    • Photoaccumulation of reduced primary electron acceptors of photosystem I of photosynthesis
    • Swarthoff T, Gast P, Amesz J, Buisman HP. 1982. Photoaccumulation of reduced primary electron acceptors of photosystem I of photosynthesis. FEBS Lett. 146:129-32
    • (1982) FEBS Lett. , vol.146 , pp. 129-132
    • Swarthoff, T.1    Gast, P.2    Amesz, J.3    Buisman, H.P.4
  • 72
    • 0033537832 scopus 로고    scopus 로고
    • X-binding niche of photosystem I - Effect of alanine and lysine replacements on photoautotrophic growth, electron transfer rates, single-turnover flash efficiency, and EPR spectral properties
    • X-binding niche of photosystem I - effect of alanine and lysine replacements on photoautotrophic growth, electron transfer rates, single-turnover flash efficiency, and EPR spectral properties. J. Biol. Chem. 274:9993-10001
    • (1999) J. Biol. Chem. , vol.274 , pp. 9993-10001
    • Vassiliev, I.R.1    Yu, J.P.2    Jung, Y.S.3    Schulz, R.4    Ganago, A.O.5
  • 73
    • 0025666994 scopus 로고
    • Thermodynamic and structural information on photosynthetic systems obtained from electroluminescence kinetics
    • Vos MH, Van Gorkom HJ. 1990. Thermodynamic and structural information on photosynthetic systems obtained from electroluminescence kinetics. Biophys. J. 58:1547-55
    • (1990) Biophys. J , vol.58 , pp. 1547-1555
    • Vos, M.H.1    Van Gorkom, H.J.2
  • 75
    • 0000106766 scopus 로고
    • Monomeric chlorophyll a enol: Evidence for its possible role as the primary electron donor in photosystem I of plant photosynthesis
    • Wasielewski MR, Norris JR, Shipman LL, Lin C-P, Svec WA. 1981. Monomeric chlorophyll a enol: evidence for its possible role as the primary electron donor in photosystem I of plant photosynthesis. Proc. Natl. Acad. Sci. USA 78:2957-61
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2957-2961
    • Wasielewski, M.R.1    Norris, J.R.2    Shipman, L.L.3    Lin, C.-P.4    Svec, W.A.5
  • 76
    • 85016544157 scopus 로고
    • Chlorophylls as functional molecules in photosynthesis. Molecular composition in vivo and physical chemistry in vitro
    • Watanabe T, Kobayashi M. 1988. Chlorophylls as functional molecules in photosynthesis. Molecular composition in vivo and physical chemistry in vitro. Nippon Kagaku Kaishi 4:383-95
    • (1988) Nippon Kagaku Kaishi , vol.4 , pp. 383-395
    • Watanabe, T.1    Kobayashi, M.2
  • 77
    • 0027265117 scopus 로고
    • Site-directed mutagenesis of the photosystem-I reaction center in chloroplasts - The proline-cysteine motif
    • Webber AN, Gibbs PB, Ward JB, Bingham SE. 1993. Site-directed mutagenesis of the photosystem-I reaction center in chloroplasts - the proline-cysteine motif. J. Biol. Chem. 268:12990-95
    • (1993) J. Biol. Chem. , vol.268 , pp. 12990-12995
    • Webber, A.N.1    Gibbs, P.B.2    Ward, J.B.3    Bingham, S.E.4
  • 78
    • 0035976006 scopus 로고    scopus 로고
    • P700: The primary electron donor of photosystem I
    • Webber AN, Lubitz W. 2001. P700: the primary electron donor of photosystem I. Biochim. Biophys. Acta 1507:61-79
    • (2001) Biochim. Biophys. Acta , vol.1507 , pp. 61-79
    • Webber, A.N.1    Lubitz, W.2
  • 79
    • 0029794447 scopus 로고    scopus 로고
    • Site-directed mutations affecting the spectroscopic characteristics and midpoint potential of the primary donor in photosystem I
    • Webber AN, Su H, Bingham SE, Kass H, Krabben L, et al. 1996. Site-directed mutations affecting the spectroscopic characteristics and midpoint potential of the primary donor in photosystem I. Biochemistry 35:12857-63
    • (1996) Biochemistry , vol.35 , pp. 12857-12863
    • Webber, A.N.1    Su, H.2    Bingham, S.E.3    Kass, H.4    Krabben, L.5
  • 80
    • 0037046990 scopus 로고    scopus 로고
    • Hydrogen bonding to P700: Site-directed mutagenesis of threonine A739 of photosystem I in Chlamydomonas reinhardtii
    • Witt H, Schlodder E, Teutloff C, Niklas J, Bordignon E, et al. 2002. Hydrogen bonding to P700: site-directed mutagenesis of threonine A739 of photosystem I in Chlamydomonas reinhardtii. Biochemistry 41:8557-69
    • (2002) Biochemistry , vol.41 , pp. 8557-8569
    • Witt, H.1    Schlodder, E.2    Teutloff, C.3    Niklas, J.4    Bordignon, E.5
  • 82
    • 0001750791 scopus 로고    scopus 로고
    • Deletion of the PsaF polypeptide modifies the environment of the redox-active phylloquinone. Evidence for unidirectionality of electron transfer in photosytem I
    • Yang F, Shen G, Schluchter WM, Zybailov B, Ganago AO, et al. 1998. Deletion of the PsaF polypeptide modifies the environment of the redox-active phylloquinone. Evidence for unidirectionality of electron transfer in photosytem I. J. Phys. Chem. 102:8288-99
    • (1998) J. Phys. Chem. , vol.102 , pp. 8288-8299
    • Yang, F.1    Shen, G.2    Schluchter, W.M.3    Zybailov, B.4    Ganago, A.O.5
  • 83
    • 0029379732 scopus 로고
    • Absence of PsaC subunit allows assembly of photosystem I core but prevents the binding of PsaD and PsaE in Synechocystis sp. PCC 6803
    • Yu JP, Smart LB, Jung YS, Golbeck J, McIntosh L. 1995. Absence of PsaC subunit allows assembly of photosystem I core but prevents the binding of PsaD and PsaE in Synechocystis sp. PCC 6803. Plant Mol. Biol. 29:331-42
    • (1995) Plant Mol. Biol. , vol.29 , pp. 331-342
    • Yu, J.P.1    Smart, L.B.2    Jung, Y.S.3    Golbeck, J.4    McIntosh, L.5
  • 86
    • 0034708663 scopus 로고    scopus 로고
    • 1 site of photosystem I. II. Structural and functional characterization of phylloquinone biosynthetic pathway mutants by electron paramagnetic resonance and electron-nuclear double resonance spectroscopy
    • 1 site of photosystem I. II. Structural and functional characterization of phylloquinone biosynthetic pathway mutants by electron paramagnetic resonance and electron-nuclear double resonance spectroscopy. J. Biol. Chem. 275:8531-39
    • (2000) J. Biol. Chem. , vol.275 , pp. 8531-8539
    • Zybailov, B.1    Van Der Est, A.2    Zech, S.G.3    Teutloff, C.4    Johnson, T.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.