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For Further Reading
W Nitschke and SM Dracheva (1995) Reaction center associated cytochromes. In: RE Blankenship, MT Madigan and CE Bauer (eds) Anoxygenic Photosynthesis, pp 776–805. Kluwer
DM Tiede and PL Dutton (1993) Electron transfer between bacterial reaction centers and mobile c-type cyto-chromes. In: JR Norris and H Deisenhofer (eds) The Photosynthetic Reaction Centers. Vol 1, pp 257–288. Acad Press
JM Olson and JP Thornber (1979) Photosynthetic reaction centers. In: RA Capaldi (ed) Membrane Proteins in Energy Transduction. pp 279–340. Dekker
References
CA MacMunn (1884) On myohaematin, an intrinsic muscle-pigment of vertebrates and invertebrates, on histohaematin, and on the spectrum of the supra-renal bodies. J Physiol 5: xxiv
D Keilin (1925) On cytochrome, a respiratory pigment, common to animals, yeast, and higher plants. Proc Roy Soc B, 98: 312–339
N Adir, HL Axelrod, P Beroza, RA Isaacson, SH Rongey, MY Okamura and G Feher (1996) Co-crystallization and characterization of the photosynthetic reaction center-cytochrome c 2 complex from Rhodobacter sphaeroides. Biochemistry 35: 2535–2547
WW Parson (1968) The role of P870 in bacterial photosynthesis. Biochim Biophys Acta 75: 248–259
WW Parson (1969) The reaction between primary and secondary electron acceptors in bacterial photosynthesis. Biochim Biophys Acta 189: 384–396
WW Parson (1969) Cytochrome photooxidation in Chromatium chromatophores. Each P870 oxidizes two cytochrome C 442 hemes. Biochim Biophys Acta 189: 397–403
RJ Shopes, LMA Levine, D Holten and CA Wraight (1987) Kinetics of oxidation of the bound cytochromes in reaction centers from Rhodopseudomonas viridis. Photosynthesis Res 12: 165–180
B Chance and M Nishimura (1960) On the mechanism of chlorophyll-cytochrome interaction: The temperature insensitivity of light-induced cytochrome oxidation in Chromatium. Proc Nat Acad Sci, USA. 46: 19–24
B Chance and D DeVault (1964) On the kinetics and quantum efficiency of the chlorophyll-cytochrome reaction. Ber Bunsenges Phys Chem 68: 723–726
D DeVault and B Chance (1966) On the kinetics and quantum efficiency of the chlorophyll-cytochrome reaction. Biophys J 6: 825–847
J Deisenhofer, O Epp, R Miki, R Huber and H Michel (1984) X-ray structure analysis of a membrane protein complex: electron density map at 3 - resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J Mol Biol 180: 385–398
SM Dracheva, LA Drachev, SM Zaberezhnaya, AA Konstantinov, A Semenov and VP Skulachev (1986) Spectral, redox and kinetic characteristics of high-potential cytochrome c hemes in Rhodopseudomonas viridis reaction center. FEBS Lett 205: 41–46
O Kaminskaya, AA Konstantinov and VA Shuvalov (19990) Low-temperature photooxidation of cytochrome c in reaction centre complexes from Rhodopseudomonas viridis. Biochim Biophys Acta 1016: 153–164
JM Ortega and P Mathis (1992) Effect of temperature of electron transfer from the tetraheme cytochrome to the primary donor in Rhodopseudomonas viridis. FEBS Lett 301: 45–48
JM Ortega and P Mathis (1993) Electron transfer from the tetraheme cytochrome to the special pair in isolated reaction centers of Rhodopseudomonas viridis. Biochemistry 32: 1141–1151
MR Gunner and B Honig (1991) Electrostatic control of midpoint potentials in the cytochrome subunit of the Rhodopseudomonas viridis reaction center. Proc Nat Acad Sci, USA 88: 9151–9155
W Nitschke and AW Rutherford (1989) Tetraheme cytochrome c subunit of Rhodopseudomonas viridis characterized by EPR. Biochemistry 28: 3161–3168
JK Blasie, M Erecinska, S Samuels and JS Leigh (1978) The structure of a cytochrome oxidase-lipid model membrane. Biochim Biophys Acta 501: 33–52
A Vermeglio, P Richaud and J Breton (1989) Orientation and assignment of the four cytochrome hemes in Rhodopseudomonas viridis reaction centers. FEBS Lett 243: 259–263
G Fritsch, S Buchanan and H Michel (1989) Assignment of cytochrome hemes in crystallized reaction centers from Rhodopseudomonas viridis. Biochim Biophys Acta 977: 157–162
G Alegria and PL Dutton (1991) I. Langmuir-Blodgett monolayer films of bacterial photosynthetic membranes and isolated reaction centers: preparation, spectrophotometric and electrochemical characterization. Biochim Biophys Acta 1057: 239–257
G Alegria and PL Dutton (1991) II. Langmuir-Blodgett monolayer films of bacterial photosynthetic membranes and isolated reaction centers: determination of the order of the hemes in the cytochrome c subunit. Biochim Biophys Acta 1057: 258–272
B Ke, TH Chaney and DW Reed (1970) The electrostatic interaction between the reaction-center bacteriochlorophyll derived from Rhodopseudomonas sphaeroides and mammalian cytochrome c and its effect on light-activated electron transport. Biochim Biophys Acta 216: 373–383
WW Parson and RK Clayton (1973) Pigment content and molar extinction coefficient of photochemical reaction center from Rhodopseudomonas sphaeroides. Biochim Biophys Acta 305: 597–609
D Rosen, MY Okamura and G Feher (1980) Interaction of cytochrome c with reaction centers of Rhodopseudomonas sphaeroides R-26: Determination of number of binding sites and dissociation constants by equilibrium analysis. Biochemistry 19: 5687–5692
RC Prince, RJ Cogdell and AR Crofts (1974) The photooxidation of horse heart cytochrome c and native cytochrome c 2 by reaction centres from Rhodopseudomonas sphaeroides R-26. Biochim Biophys Acta 347: 1–13
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(2003). The Secondary Electron Donor of Photosynthetic Bacteria the Cytochromes. In: Photosynthesis. Advances in Photosynthesis and Respiration, vol 10. Springer, Dordrecht. https://doi.org/10.1007/0-306-48136-7_10
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DOI: https://doi.org/10.1007/0-306-48136-7_10
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