메뉴 건너뛰기




Volumn 59, Issue 2-3, 1999, Pages 147-157

Electron transfer between cytochrome c2 and the tetraheme cytochrome c in Rhodopseudomonas viridis

Author keywords

Flash absorption spectroscopy; Purple bacteria; Reaction center

Indexed keywords

RHODOPSEUDOMONAS VIRIDIS;

EID: 0032784675     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1023/a:1006149621029     Document Type: Article
Times cited : (20)

References (45)
  • 2
    • 0022364841 scopus 로고
    • Orientation of the chromophores in the reaction center of Rhodopseudomonas viridis. Comparison of low-temperature linear dichroism spectra with a model derived from x-ray crystallography
    • Breton J (1985) Orientation of the chromophores in the reaction center of Rhodopseudomonas viridis. Comparison of low-temperature linear dichroism spectra with a model derived from x-ray crystallography. Biochim Biophys Acta 810: 235-245
    • (1985) Biochim Biophys Acta , vol.810 , pp. 235-245
    • Breton, J.1
  • 3
    • 0017883063 scopus 로고
    • Molar extinction coefficients and other properties of an improved reaction center preparation from Rps. viridis
    • Clayton RK and Clayton B (1978) Molar extinction coefficients and other properties of an improved reaction center preparation from Rps. viridis. Biochim Biophys Acta 501: 478-487
    • (1978) Biochim Biophys Acta , vol.501 , pp. 478-487
    • Clayton, R.K.1    Clayton, B.2
  • 4
    • 70449138041 scopus 로고
    • Kinetic studies of pigment synthesis by non-sulfur purple bacteria
    • Cohen-Bazire G, Sistrom WR and Stanier RY (1957) Kinetic studies of pigment synthesis by non-sulfur purple bacteria. J Cell Comp Physiol 49: 25-68
    • (1957) J Cell Comp Physiol , vol.49 , pp. 25-68
    • Cohen-Bazire, G.1    Sistrom, W.R.2    Stanier, R.Y.3
  • 5
    • 0021874143 scopus 로고
    • The pathway of cyclic electron transport in chromatophores of Chromatium vinosum. Evidence for a Q-cycle mechanism
    • Coremans JMCC, Van der Wal HN, Van Grondelle R, Amesz J and Knaff DB (1985) The pathway of cyclic electron transport in chromatophores of Chromatium vinosum. Evidence for a Q-cycle mechanism. Biochim Biophys Acta 807: 134-142
    • (1985) Biochim Biophys Acta , vol.807 , pp. 134-142
    • Coremans, J.M.C.C.1    Van Der Wal, H.N.2    Van Grondelle, R.3    Amesz, J.4    Knaff, D.B.5
  • 6
    • 48749143707 scopus 로고
    • The electrochemical domain of photosynthesis
    • Crofts AR and Wraight CA (1983) The electrochemical domain of photosynthesis. Biochim Biophys Acta 726: 149-185
    • (1983) Biochim Biophys Acta , vol.726 , pp. 149-185
    • Crofts, A.R.1    Wraight, C.A.2
  • 7
    • 0001104663 scopus 로고
    • The role of quinone pool in the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides. a modified Q-cycle mechanism
    • Crofts AR, Meinhard SW, Jones KR and Snozzi M (1983) The role of quinone pool in the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides. A modified Q-cycle mechanism. Biochim Biophys Acta 723: 202-218
    • (1983) Biochim Biophys Acta , vol.723 , pp. 202-218
    • Crofts, A.R.1    Meinhard, S.W.2    Jones, K.R.3    Snozzi, M.4
  • 8
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 a resolution
    • Deisenhofer J, Epp O, Miki K, Huber R and Michel H (1985) Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 A resolution. Nature 318:618-624
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 9
    • 0028957690 scopus 로고
    • Crystallographic refinement at 2.3 Å resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis
    • Deisenhofer J, Epp O, Miki K and Michel H (1995) Crystallographic refinement at 2.3 Å resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis. J Mol Biol 246: 429-457
    • (1995) J Mol Biol , vol.246 , pp. 429-457
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Michel, H.4
  • 12
    • 0031033675 scopus 로고    scopus 로고
    • 2 in electron transfer complexes with the photosynthetic reaction center of Rhodobacter sphaeroides: Optical linear dichroism and EPR
    • 2 in electron transfer complexes with the photosynthetic reaction center of Rhodobacter sphaeroides: Optical linear dichroism and EPR. Biochemistry 36: 1428-1440
    • (1997) Biochemistry , vol.36 , pp. 1428-1440
    • Drepper, F.1    Mathis, P.2
  • 13
    • 0010572378 scopus 로고
    • Reaction-center-driven cytochrome interactions in electron and proton translocation and energy coupling
    • Clayton RK and Sistrom WR (eds) Plenum Press, New York
    • Dutton PL and Prince RC (1978) Reaction-center-driven cytochrome interactions in electron and proton translocation and energy coupling. In: Clayton RK and Sistrom WR (eds) The Photosynthetic Bacteria, pp 525-570. Plenum Press, New York
    • (1978) The Photosynthetic Bacteria , pp. 525-570
    • Dutton, P.L.1    Prince, R.C.2
  • 15
    • 0000494859 scopus 로고
    • Assignment of cytochrome hemes in crystallized reaction center from Rhodopseudomonas viridis
    • Fritzsch G, Buchanan S and Michel H (1989) Assignment of cytochrome hemes in crystallized reaction center from Rhodopseudomonas viridis. Biochim Biophys Acta 977: 157-162
    • (1989) Biochim Biophys Acta , vol.977 , pp. 157-162
    • Fritzsch, G.1    Buchanan, S.2    Michel, H.3
  • 16
    • 0027374987 scopus 로고
    • The photoinduced cyclic electron transfer in whole cells of Rhodopseudomonas viridis
    • Garcia D, Richaud P and Verméglio A (1993) The photoinduced cyclic electron transfer in whole cells of Rhodopseudomonas viridis. Biochim Biophys Acta 1144: 295-301
    • (1993) Biochim Biophys Acta , vol.1144 , pp. 295-301
    • Garcia, D.1    Richaud, P.2    Verméglio, A.3
  • 17
    • 0029967413 scopus 로고    scopus 로고
    • Complete coordination of the four Fe-S centers of the β subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants laking the highest or lowest potential [4Fe-4S] clusters
    • Guigliarelli B, Magalon A, Asso M, Bertrand P, Frixon C, Giordano G and Blasco F (1996) Complete coordination of the four Fe-S centers of the β subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants laking the highest or lowest potential [4Fe-4S] clusters. Biochemistry 35: 4828-4836
    • (1996) Biochemistry , vol.35 , pp. 4828-4836
    • Guigliarelli, B.1    Magalon, A.2    Asso, M.3    Bertrand, P.4    Frixon, C.5    Giordano, G.6    Blasco, F.7
  • 18
    • 0027463017 scopus 로고
    • Synechocystis 6803 plastocyanin isolated from both the cyanobacterium and E. coli transformed cells are identical
    • Hervás M, Navarro F, Navarro JA, Chávez S, Díaz A, Florencio FJ and De la Rosa MA (1993) Synechocystis 6803 plastocyanin isolated from both the cyanobacterium and E. coli transformed cells are identical. FEBS Lett 319: 257-260
    • (1993) FEBS Lett , vol.319 , pp. 257-260
    • Hervás, M.1    Navarro, F.2    Navarro, J.A.3    Chávez, S.4    Díaz, A.5    Florencio, F.J.6    De La Rosa, M.A.7
  • 19
    • 0030011855 scopus 로고    scopus 로고
    • Kinetics of photo-induced electron transfer from high-potential iron-sulfur protein to the photosynthetic reaction center of the purple phototroph Rhodoferax fermentons
    • Hochkoeppler A, Zannoni D, Ciurli S, Meyer TE, Cusanovich MA and Tollin G (1996) Kinetics of photo-induced electron transfer from high-potential iron-sulfur protein to the photosynthetic reaction center of the purple phototroph Rhodoferax fermentons. Proc Natl Acad Sci 93: 6998-7002
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 6998-7002
    • Hochkoeppler, A.1    Zannoni, D.2    Ciurli, S.3    Meyer, T.E.4    Cusanovich, M.A.5    Tollin, G.6
  • 20
    • 0025922846 scopus 로고
    • Reaction of cytochrome Q with photosynthetic reaction center from Rhodopseudomonas viridis
    • Knaff DB, Willie A, Long JE, Kriauciunas A, Durham B and Millet F (1991) Reaction of cytochrome Q with photosynthetic reaction center from Rhodopseudomonas viridis. Biochemistry 30: 1304-1310
    • (1991) Biochemistry , vol.30 , pp. 1304-1310
    • Knaff, D.B.1    Willie, A.2    Long, J.E.3    Kriauciunas, A.4    Durham, B.5    Millet, F.6
  • 21
    • 0022004980 scopus 로고
    • Electron transfer in chemistry and biology
    • Marcus RA and Sutin N (1985) Electron transfer in chemistry and biology. Biochim Biophys Acta 811: 265-322
    • (1985) Biochim Biophys Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 22
    • 0038760021 scopus 로고
    • Cytochromes functionally associated to photochemical reaction centers in Rhodopseudomonas patustris and Rhodopseudomonas acidophita
    • Matsuura K and Shimada K (1986) Cytochromes functionally associated to photochemical reaction centers in Rhodopseudomonas patustris and Rhodopseudomonas acidophita. Biochim Biophys Acta 852: 9-18
    • (1986) Biochim Biophys Acta , vol.852 , pp. 9-18
    • Matsuura, K.1    Shimada, K.2
  • 23
    • 33847510887 scopus 로고    scopus 로고
    • Transfert cyclique photo-induit d'électrons chez les bactéries photosynthétiques pourpres
    • PhD Thesis, University of Provence (Marseille)
    • Menin L (1997) Transfert cyclique photo-induit d'électrons chez les bactéries photosynthétiques pourpres. Rôle de la HiPIP et des cytochromes de type c. PhD Thesis, University of Provence (Marseille)
    • (1997) Rôle de la HiPIP et des Cytochromes de Type C
    • Menin, L.1
  • 24
    • 0027180799 scopus 로고
    • Kinetics of photooxidation of soluble cytochromes, HiPIP and azurin by the photosynthetic reaction center of the purple phototrophic bacterium Rhodopseudomonas viridis
    • Meyer TE, Bartsch RG, Cusanovich MA and Tollin G (1993) Kinetics of photooxidation of soluble cytochromes, HiPIP and azurin by the photosynthetic reaction center of the purple phototrophic bacterium Rhodopseudomonas viridis. Biochemistry 32:4719-4726
    • (1993) Biochemistry , vol.32 , pp. 4719-4726
    • Meyer, T.E.1    Bartsch, R.G.2    Cusanovich, M.A.3    Tollin, G.4
  • 25
    • 0026763765 scopus 로고
    • Engineering protein structure for electron transfer function in photosynthetic reaction centers
    • Moser CC and Dutton PL (1992) Engineering protein structure for electron transfer function in photosynthetic reaction centers. Biochim Biophys Acta 1101: 171-176
    • (1992) Biochim Biophys Acta , vol.1101 , pp. 171-176
    • Moser, C.C.1    Dutton, P.L.2
  • 27
    • 0001228592 scopus 로고
    • Reaction center associated cytochromes
    • Blankenship RE, Madigan MT and Bauer CE (eds) Kluwer Academic Publishers, Dordrecht, the Netherlands
    • Nitschke W and Dracheva SM (1995) Reaction center associated cytochromes. In: Blankenship RE, Madigan MT and Bauer CE (eds) Anoxygenic Photosynthetic Bacteria, pp 776-805. Kluwer Academic Publishers, Dordrecht, the Netherlands
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 776-805
    • Nitschke, W.1    Dracheva, S.M.2
  • 28
    • 0000160456 scopus 로고
    • Tetraheme cytochrome c subunit of Rhodopseudomonas viridis characterized by EPR
    • Nitschke W and Rutherford AW (1989) Tetraheme cytochrome c subunit of Rhodopseudomonas viridis characterized by EPR. Biochemistry 28: 3161-3168
    • (1989) Biochemistry , vol.28 , pp. 3161-3168
    • Nitschke, W.1    Rutherford, A.W.2
  • 29
    • 0013796284 scopus 로고
    • Energy transfer and cytochrome function in a new type of photosynthetic bacterium
    • Olson JM and Nadler KD (1965) Energy transfer and cytochrome function in a new type of photosynthetic bacterium. Photochem Photobiol 4: 783-791
    • (1965) Photochem Photobiol , vol.4 , pp. 783-791
    • Olson, J.M.1    Nadler, K.D.2
  • 30
    • 0031025928 scopus 로고    scopus 로고
    • Very fast electron transfer from cytochrome to the bacterial photosynthetic reaction center at low temperature
    • Onega JM, Dohse B, Oesterhelt D and Mathis P (1997) Very fast electron transfer from cytochrome to the bacterial photosynthetic reaction center at low temperature. FEBS Lett 401: 153-157
    • (1997) FEBS Lett , vol.401 , pp. 153-157
    • Onega, J.M.1    Dohse, B.2    Oesterhelt, D.3    Mathis, P.4
  • 31
    • 0027535989 scopus 로고
    • Electron transfer from the tetraheme cytochrome to the special pair in isolated reaction centers of Rhodopseudomonas viridis
    • Ortega JM and Mathis P (1993) Electron transfer from the tetraheme cytochrome to the special pair in isolated reaction centers of Rhodopseudomonas viridis. Biochemistry 32: 1141-1151
    • (1993) Biochemistry , vol.32 , pp. 1141-1151
    • Ortega, J.M.1    Mathis, P.2
  • 32
    • 0031910467 scopus 로고    scopus 로고
    • Low-temperature electron transfer from cytochrome to the special pair in Rhodopseudomonas viridis: Role of the L162 residue
    • Ortega JM, Dohse B, Oesterhelt D and Mathis P (1998) Low-temperature electron transfer from cytochrome to the special pair in Rhodopseudomonas viridis: Role of the L162 residue. Biophys J74: 1135-1148
    • (1998) Biophys J , vol.74 , pp. 1135-1148
    • Ortega, J.M.1    Dohse, B.2    Oesterhelt, D.3    Mathis, P.4
  • 33
    • 0032566342 scopus 로고    scopus 로고
    • Interaction site for soluble cytochromes on the tetraheme cytochrome subunit bound to the bacterial photosynthetic reaction center mapped by site-directed mutagenesis
    • Osyczka A, Nagashima KVP, Sogabe S, Miki K, Yoshida M, Shimada K and Matsuura K (1998) Interaction site for soluble cytochromes on the tetraheme cytochrome subunit bound to the bacterial photosynthetic reaction center mapped by site-directed mutagenesis. Biochemistry 37: 11732-11744
    • (1998) Biochemistry , vol.37 , pp. 11732-11744
    • Osyczka, A.1    Nagashima, K.V.P.2    Sogabe, S.3    Miki, K.4    Yoshida, M.5    Shimada, K.6    Matsuura, K.7
  • 34
    • 0018087476 scopus 로고
    • Redox potentials of the photosynthetic bacterial cytochromes Q and the structural bases for variability
    • Pettigrew GW, Bartsch R, Meyer T and Kamen MD (1978) Redox potentials of the photosynthetic bacterial cytochromes Q and the structural bases for variability. Biochim Biophys Acta 503: 509-523
    • (1978) Biochim Biophys Acta , vol.503 , pp. 509-523
    • Pettigrew, G.W.1    Bartsch, R.2    Meyer, T.3    Kamen, M.D.4
  • 35
    • 0031856790 scopus 로고    scopus 로고
    • Time-resolved electron transfer at the donor side of Rhodopseudomonas viridis photosynthetic reaction centers in whole cells
    • Rappaport F, Béai D, Verméglio A and Joliot P (1998) Time-resolved electron transfer at the donor side of Rhodopseudomonas viridis photosynthetic reaction centers in whole cells. Photosynth Res 55: 317-323
    • (1998) Photosynth Res , vol.55 , pp. 317-323
    • Rappaport, F.1    Béai, D.2    Verméglio, A.3    Joliot, P.4
  • 36
    • 0029088458 scopus 로고
    • In vivo participation of a high potential iron-sulfur protein as electron donors to photochemical reaction centers of Rubrivivax getatinosus
    • Schoepp B, Parot P, Menin L, Gaillard P, Richaud P and Verméglio A (1995) In vivo participation of a high potential iron-sulfur protein as electron donors to photochemical reaction centers of Rubrivivax getatinosus. Biochemistry 34: 11736-11742
    • (1995) Biochemistry , vol.34 , pp. 11736-11742
    • Schoepp, B.1    Parot, P.2    Menin, L.3    Gaillard, P.4    Richaud, P.5    Verméglio, A.6
  • 37
    • 33847501624 scopus 로고    scopus 로고
    • EPR studies on the interaction between HiPIP and the photosynthetic membrane in the purple bacterium Rubrivivax getatinosus
    • in press
    • Schoepp B, Riedel A, Verméglio A, Kappl R and Nitschke W (1998) EPR studies on the interaction between HiPIP and the photosynthetic membrane in the purple bacterium Rubrivivax getatinosus. Eur J Biochem (in press)
    • (1998) Eur J Biochem
    • Schoepp, B.1    Riedel, A.2    Verméglio, A.3    Kappl, R.4    Nitschke, W.5
  • 39
    • 0000859560 scopus 로고
    • Kinetics of oxidation of the bound cytochromes in reaction centers from Rps. viridis
    • Shopes RJ, Levine LMA, Holten D and Wraight CA (1987) Kinetics of oxidation of the bound cytochromes in reaction centers from Rps. viridis. Photosynth Res 12: 165-180.
    • (1987) Photosynth Res , vol.12 , pp. 165-180
    • Shopes, R.J.1    Levine, L.M.A.2    Holten, D.3    Wraight, C.A.4
  • 42
    • 0017387066 scopus 로고
    • Function and properties of soluble c-type cytochrome c-551 in secondary electron transport in whole cells of Chromatium vinosum as studied with flash spectroscopy
    • Van Grondelle R, Duysens LMN, Van der Wel JA and Van der Wal HN (1977) Function and properties of soluble c-type cytochrome c-551 in secondary electron transport in whole cells of Chromatium vinosum as studied with flash spectroscopy. Biochim Biophys Acta 461: 188-201
    • (1977) Biochim Biophys Acta , vol.461 , pp. 188-201
    • Van Grondelle, R.1    Duysens, L.M.N.2    Van Der Wel, J.A.3    Van Der Wal, H.N.4
  • 43
    • 0027754117 scopus 로고
    • 2 to the primary donor of Rhodobacter sphaeroides reaction centers. a temperature dependence study
    • 2 to the primary donor of Rhodobacter sphaeroides reaction centers. A temperature dependence study. Biochemistry 32: 13245-13253
    • (1993) Biochemistry , vol.32 , pp. 13245-13253
    • Venturoli, G.1    Mallardi, A.2    Mathis, P.3
  • 44
    • 0039582443 scopus 로고
    • Orientation and assignment of the four cytochromes hemes in Rhodopseudomonas viridis reaction centers
    • Verméglio A, Richaud P and Breton J (1989) Orientation and assignment of the four cytochromes hemes in Rhodopseudomonas viridis reaction centers. FEBS Lett 243: 259-263
    • (1989) FEBS Lett , vol.243 , pp. 259-263
    • Verméglio, A.1    Richaud, P.2    Breton, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.