The General Kinetic Model of Electron Transfer in Photosynthetic Reaction Centers Activated by Multiple Flashes

Photochemistry and Photobiology

Volumn 67, Issue 6, 1998, Pages 683-699

  Shinkarev, Vladimir P ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEOBACTERIA;

ARTICLE; CHEMICAL MODEL; ELECTRON TRANSPORT; KINETICS; LIGHT; METABOLISM; PHOTOSYNTHESIS; RADIATION EXPOSURE; RHODOBACTER SPHAEROIDES;

ELECTRON TRANSPORT; KINETICS; LIGHT; MODELS, CHEMICAL; PHOTOSYNTHETIC REACTION CENTER COMPLEX PROTEINS; RHODOBACTER SPHAEROIDES;

EID: 0032085285     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.1998.tb09474.x     Document Type: Article

References (90)

1. Crofts, A. R. and C. A. Wraight (1983) The electrochemical domain of photosynthesis. Biochim. Biophys. Acta 726, 149-185.
2. Gunner, M. R. (1991) The reaction center protein from purple bacteria: structure and function. Curr. Top. Bioenerg. 16, 319-367.
3. Shinkarev, V. P. and C. A. Wraight (1993) Electron and proton transfer in the acceptor quinone complex of reaction centers of phototrophic bacteria. In The Photosynthetic Reaction Center, Vol. 1 (Edited by J. Deisenhofer and J. Norris), pp. 193-255. Academic Press, New York.
4. B in reaction centers from photosynthetic bacteria. In Anoxygenic Photosynthetic Bacteria (Edited by R. E. Blankenship, M. T. Madigan and C. E. Bauer), pp. 577-593. Kluwer, Dordrecht.
5. Deisenhofer, J., O. Epp, K. Miki, R. Huber and H. Michel (1984) X-ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromatophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J. Mol. Biol. 180, 385-398.
6. Deisenhofer, J. and H. Michel (1989) The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis. EMBO J. 8, 2149-2170.
7. Deisenhofer, J., O. Epp, I. Sinning and H. Michel (1995) Crystallographic refinement at 2.3-angstrom resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis. J. Mol. Biol. 246, 429-457.
8. Allen, J. P., G. Feher, T. O. Yeates, H. Komiya and D. C. Rees (1987) Structure of the reaction center from Rhodobacter sphaeroides R-26: the cofactors. Proc. Natl. Acad. Sci. USA 84, 5730-5734.
9. Feher, G., J. P. Allen, M. Y. Okamura and D. C. Rees (1989) Structure and function of bacterial photosynthetic reaction centers. Nature 339, 111-116.
10. El-Kabbani, O., C. H. Chang, D. Tiede, J. Norris and M. Schiffer (1991) Comparison of reaction centers from Rhodobacter sphaeroides and Rhodopseudomonas viridis: overall architecture and protein-pigment interactions. Biochemistry 30, 5361-5369.
11. Ermler, U., G. Fritzsch, S. K. Buchanan and H. Michel (1994) Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: cofactors and protein-cofactor interactions. Structure 2, 925-936.
12. Dutton, P. L. and R. G. Prince (1978) Reaction-center-driven cytochrome interactions in electron and proton translocation and energy coupling. In The Photosynthetic Bacteria (Edited by R. K. Clayton and W. R. Sistrom), pp. 525-571. Plenum Press, New York.
13. 2 oxidoreductase in Rhodopseudomonas sphaeroides chromatophores. Biochim. Biophys. Acta 637, 512-522.
14. + binding by bacterial photosynthetic reaction centers: influences of the redox states of the acceptor quinones and primary donor. Biochim. Biophys. Acta 934, 329-347.
15. Sebban, P., P. Maróti and D. K. Hanson (1995) Electron and proton transfer to the quinones in bacterial photosynthetic reaction centers: insight from combined approaches of molecular genetics and biophysics. Biochimie 77, 677-694.
16. Wraight, C. A. (1981) Oxidation-reduction physical chemistry of the acceptor quinone complex in bacterial photosynthetic reaction centers: evidence for a new model of herbicide activity. Isr. J. Chem. 21, 348-354.
17. Wraight, C. A. and R. R. Stein (1983) Bacterial reaction centers as a model for photosystem II. Turnover of the secondary acceptor quinone. In The Oxygen Evolving Systems of Photosynthesis (Edited by Y. Inoue et al.), pp. 383-392. Academic Press, Tokyo.
18. Shinkarev, V. P. and C. A. Wraight (1997) The interaction of quinone and detergent with reaction centers of purple bacteria. I. Slow quinone exchange between reaction center micelles and pure detergent micelles. Biophys. J. 72, 2304-2319.
19. Shinkarev, V. P., A. A. Kononenko and A. B. Rubin (1984) On molecular mechanisms of electron transfer in the system of quinone acceptors of purple bacteria photosynthetic RCs. Biol. Membr. (USSR) 2, 640-650.
20. Shinkarev, V. P., V. D. Sled and A. B. Rubin (1984) On mechanism of o-phenanthroline effect on electron transport in purple bacteria. Biophysics (USSR) 29, 595-600.
21. Shinkarev, V. P., M. I. Verkhovsky, B. S. Kaurov and A. B. Rubin (1981) The kinetic model of two-electron gate in photosynthetic RCs of purple bacteria. Mol. Biol. (USSR) 15, 1069-1082.
22. -. Biochim. Biophys. Acta 765, 405-409.
23. Tandori, J., L. Nagy and P. Maróti (1991) Semiquinone oscillations as a probe of quinone/herbicide binding in bacterial reaction centers. Photosynthetica 25, 159-166.
24. Wraight, C. A. (1977) Electron acceptors of photosynthetic bacterial reaction centers. Direct observation of oscillatory behavior suggesting two closely equivalent ubiquinones. Biochim. Biophys. Acta 459, 525-531.
25. Verméglio, A. (1977) Secondary electron transfer in reaction centers of Rhodopseudomonas sphaeroides. Out-of-phase periodicity of two for the formation of ubisemiquinone and fully reduced ubiquinone. Biochim. Biophys. Acta 459, 516-524.
26. DeGrooth, B. G., R. van Grondelle, J. C. Romijn and M. P. J. Pulles (1978) The mechanism of reduction of the ubiquinone pool in photosynthetic bacteria at different redox potentials. Biochim. Biophys. Acta 503, 480-490.
27. Barouch, Y. and R. K. Clayton (1977) Ubiquinone reduction and proton uptake by chromatophores of Rhodopseudomonas sphaeroides R-26. Periodicity of two in consecutive light flashes. Biochim. Biophys. Acta 462, 785-790.
28. + binding coupled to secondary electron transfer in the quinone acceptor complex. Biochim. Biophys. Acta 548, 309-327.
29. + uptake and generation of electric potential in chromatophores of purple bacteria. Biol. Sci. (USSR) 8, 35-37.
30. Kaminskaya, O. P., L. A. Drachev, A. A. Konstantinov, A. Yu. Semenov and V. P. Skulachev (1986) Electrogenic reduction of the secondary quinone acceptor in chromatophores of Rhodospirillum rubrum. FEBS Lett. 202, 224-228.
31. 1 complex of Rhodobacter sphaeroides chromatophores. Biochim. Biophys. Acta 973, 189-197.
32. Dracheva, S. M., L. A. Drachev, A. A. Konstantinov, A. Yu. Semenov, V. P. Skulachev, A. M. Arutjunjan, V. A. Shuvalov and S. M. Zaberezhnaya (1988) Electrogenic steps in the redox reactions catalyzed by photosynthetic reaction center complex from Rhodopseudomonas viridis. Eur. J. Biochem. 171, 253-264.
33. Mamedov, M. D., V. P. Shinkarev, M. I. Verkhovsky and A. Yu. Semenov (1990) Protonation of secondary quinone in proteoliposomes with reaction centers of Rhodobacter sphaeroides. Biol. Membr. (USSR) 7, 730-735.
34. Verméglio, A. and R. K. Clayton (1977) Kinetics of electron transfer between the primary and secondary electron acceptors in reaction center from Rhodopseudomonas sphaeroides. Biochim. Biophys. Acta 461, 159-165.
35. Diner, B. A., C. C. Shenck and C. DeVitry (1984) Effect of inhibitors, redox state and isoprenoid chain on the affinity of ubiquinone for the secondary acceptor binding site in the reaction centers of photosynthetic bacteria. Biochim. Biophys. Acta 776, 9-20.
36. Verméglio, A. (1982) Electron transfer between primary and secondary electron acceptors in chromatophores and reaction centers of photosynthetic bacteria. In Function of Quinones in Energy Conserving Systems (Edited by B. L. Trumpower), pp. 169-180. Academic Press, New York.
37. 50 reduction on consecutive light flashes. FEBS Lett. 101, 201-206.
38. Sled', V. D., M. I. Verkhovsky, V. P. Shinkarev, N. P. Grishanova and B. S. Kaurov (1983) Interaction of redox mediators with chromatophores of photosynthetic bacteria Rhodospirillum rubrum. Mol. Biol. (USSR) 7, 33-41.
39. Takahashi, E. and C. A. Wraight (1996) Potentiation of proton transfer function by electrostatic interactions in photosynthetic reaction centers from Rhodobacter sphaeroides: first results from site-directed mutation of the H-subunit. Proc. Natl. Acad. Sci. USA 93, 2640-2645.
40. Wraight, C. A. (1978) Iron-quinone interactions in the electron acceptor region of bacterial photosynthetic reaction center. FEBS Lett. 93, 283-288.
41. Okamura, M. Y., G. Feher and N. Nelson (1982) Reaction centers in bacteria and green plants. In Photosynthesis. Energy Conversion by Plants and Bacteria (Edited by Govindjee), pp. 195-274. Academic Press, New York.
42. Verméglio, A. and J. M. Carrier (1984) Photoinhibition by flash and continuous light of oxygen uptake by intact photosynthetic bacteria. Biochim. Biophys. Acta 764, 233-238.
43. Leibl, W. and J. Breton (1991) Kinetic properties of the acceptor quinone complex in Rhodopseudomonas viridis. Biochemistry 30, 9634-9642.
44. Osváth, S., G. Laczkó P. Sebban and P. Maróti (1996) Electron transfer in reaction centers of Rhodobacter sphaeroides and Rhodobacter capsulatus monitored by fluorescence of the bacteriochlorophyll dimer. Photosynth. Res. 47, 41-49.
45. Verméglio, A. and P. Joliot (1984) Light induced absorption changes in intact cells of Rhodopseudomonas sphaeroides. Evidence for interaction between photosynthetic and respiratory electron transfer chains. Biochim. Biophys. Acta 764, 226-232.
46. 6 and f in isolated plastoquinol-plastocyanin oxidoreductase driven by photochemical reaction centers from Rhodopseudomonas sphaeroides. J. Biol. Chem. 257, 3379-3381.
47. B-binding site of Rhodobacter sphaeroides reaction center. Biochemistry 31, 855-866.
48. Maróti, P., D. K. Hanson, L. Baciou, M. Schiffer and P. Sebban (1994) Proton conduction within the reaction centers of Rhodobacter capsulatus: the electrostatic role of the protein. Proc. Natl. Acad. Sci. USA 91, 5617-5621.
49. B-pocket in reaction centers of Rhodobacter sphaeroides. Photosynth. Res. 45, 135-146.
50. Svensson, B., C. Etchebest, P. Tuffery, P. van Kan, J. Smith and S. Styring (1996) A model for the photosystem II reaction center core including the structure of the primary donor P680. Biochemistry 35, 14486-14502.
51. Xiong, J., S. Subramaniam and Govindjee (1996) Modeling of the D1/D2 proteins and cofactors of the photosystem II reaction center: implications for herbicide and bicarbonate binding. Protein Sci. 5, 2054-2073.
52. Takahashi, E. and C. A. Wraight (1994) Molecular genetic manipulation and characterization of mutant photosynthetic reaction centers from purple nonsulfur bacteria. Adv. Mol. Cell Biol. 10, 197-251.
53. - recombination kinetics in reaction centers from Rhodopseudomonas viridis: the effects of pH and temperature. Biochim. Biophys. Acta 974, 54-65.
54. Parot, P., J. Thiery and A. Vermeglio (1987) Charge recombination at low temperature in photosynthetic bacteria reaction centers: evidence for two conformational states. Biochim. Biophys. Acta 893, 534-543.
55. Kleinfeld, D., M. Y. Okamura and G. Feher (1984) Electron-transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: evidence for light-induced structural changes. Biochemistry 23, 5780-5886.
56. Rubin, A. B. and V. P. Shinkarev (1984) Electron Transfer in Biological Systems. Nauka, Moscow.
57. -. Biochim. Biophys. Acta 766, 126-140.
58. Shinkarev, V. P., L. A. Drachev, M. D. Mamedov, A. Ja. Mulk-idjanian, A. Yu. Semenov and M. I. Verkhovsky (1993) Effect of pH and ionic strength on kinetics of generation of electric potential due to secondary quinone protonation in chromatophores of Rhodobacter sphaeroides. Biochim. Biophys. Acta 1144, 285-294.
59. Tiede, D. M., J. Vázquez, J. Córdova and P. A. Marone (1996) Time-resolved electrochromism associated with the formation of quinone anions in the Rhodobacter sphaeroides R26 reaction center. Biochemistry 35, 10763-10775.
60. Rongey, S. H., M. L. Paddock, G. Feher and M. Y. Okamura (1993) Pathway of proton transfer in bacterial reaction centers: second-site mutation Asn-M44 → Asp restores electron and proton transfer in reaction centers from the photosynthetically deficient Asp-L213 → Asn mutant of Rhodobacter sphaeroides. Proc. Natl. Acad. Sci. USA 90, 1325-1329.
61. Sled', V. D., V. P. Shinkarev, M. I. Verkhovsky, N. P. Grishanova and A. B. Rubin (1985) Kinetics characteristics of quinone interaction with photosynthetic RCs in chromatophore membranes of nonsulphur purple bacteria Rhodospirillum rubrum. Biol. Membr. (USSR) 2, 575-587.
62. Shinkarev, V. P. (1990) Function of Quinones in Bacterial Photosynthesis. VINITI, Moscow.
63. B leaves the reaction center. Biochim. Biophys. Acta 1016, 289-292.
64. Crofts, A. R., S. W. Meinhardt, K. R. Jones and M. Snozzi (1983) The role of the quinone pool in the cyclic electron transport chain of Rhodopseudomonas sphaeroides: a modified Q-cycle mechanism. Biochim. Biophys. Acta 723, 202-218.
65. 2 oxidoreductase? Photosynth. Res. 22, 69-87.
66. 1 complex in Rhodobacter sphaeroides chromatophores under oxidizing conditions. FEBS Lett. 245, 43-46.
67. Venturoli, G., J. G. Fernandez-Velasco, A. R. Crofts and B. A. Melandri (1986) Demonstration of a collisional interaction of ubiquinol with the ubiquinol-cytochrome c oxidoreductase complex in chromatophores from Rhodobacter sphaeroides. Biochim. Biophys. Acta 851, 340-352.
68. Takamiya, K. I. and P. L. Dutton (1979) Ubiquinone in Rhodopseudomonas sphaeroides. Biochim. Biophys. Acta 546, 1-16.
69. Garcia, A. F., G. Venturoli, N. Gad'on, S. Fernandez-Velasco, B. A. Melandri and G. Drews (1987) The adaptation of the electron transfer chain of Rhodopseudomonas capsulata to the different light intensities. Biochim. Biophys. Acta 890, 335-345.
70. Venturoli, G., J. G. Fernandez-Velasco, A. R. Crofts and B. A. Melandri (1988) The effect of the size of the quinone pool on the electrogenic reactions in the ubiquinol-cytochrome c oxidoreductase of Rhodobacter capsulatus. Pool behavior at the quinone reductase site. Biochim. Biophys. Acta 935, 258-272.
71. Venediktov, P. S., A. B. Rubin, M. I. Freidlin and V. P. Shinkarev (1979) Asymptotic analysis of the functioning of multienzyme complex performing electron transfer. Biophysics (USSR) 24, 688-693.
72. Wraight, C. A. and R. K. Clayton (1973) The absolute quantum efficiency of bacteriochlorophyll photooxidation in reaction centers of Rhodopseudomonas sphaeroides. Biochim. Biophys. Acta 333, 246-260.
73. Feller, W. (1970) An Introduction to the Probability Theory and Its Applications. Vol. 1. John Wiley and Sons, New York.
74. Stein, R. R., A. L. Castellvi, J. P. Bogacz and C. A. Wraight (1984) Herbicide-quinone competition in the acceptor complex of photosynthetic reaction centers from Rhodopseudomonas sphaeroides: a bacterial model for PSII-herbicide activity in plants. J. Cell. Biochem. 24, 243-259.
75. Shinkarev, V. P., M. I. Verkhovsky, Ja. Sabo, N. I. Zakharova, N. K. Seyfullina and A. A. Kononenko (1990) Characterization of photosynthetic cytochrome-containing reaction center preparations from Chromatium minutissimum. Biol. Membr. (USSR) 7, 368-381.
76. Sled', V. D., M. I. Verkhovsky, V. P. Shinkarev, P. T. Mominov, V. N. Verkhoturov and K. N. Timofeev (1985) pH-dependence of the redox equilibrium between primary and secondary quinone acceptors of the photosynthetic RCs in chromatophores of the purple bacteria. Biol Membr. (USSR) 2, 1016-1021.
77. Shinkarev, V. P., M. I. Verkhovsky and N. I. Zakharova (1989) Effect of amino acid residues protonation on electron transfer between quinone acceptors in RCs of purple bacteria Rhodobacter sphaeroides. Biokhimia (USSR) 54, 256-264.
78. - stabilization in herbicide-resistant mutants from the purple bacterium Rhodopseudomonas viridis. Biochemistry 30, 9110-9116.
79. A site. Chem. Phys. 197, 355-366.
80. Verkhovsky, M. I., B. S. Kaurov, A. B. Rubin and V. P. Shinkarev (1981) Kinetics of ubisemiquinone redox changes in primary reactions of bacteria photosynthesis. Mol. Biol. (USSR) 15, 589-600.
81. Mulkidjanian, A. Ya., V. P. Shinkarev, M. I. Verkhovsky and B. S. Kaurov (1986) A study of the kinetic properties of the stable semiquinone of the reaction-center secondary acceptor in chromatophores of non-sulfur bacteria. Biochim. Biophvs. Acta 849, 150-161.
82. Lide, D. R. (ed.) (1991) Handbook of Chemistry and Physics, 72nd ed., pp. 8-19. CRC Press, Boca Raton, FL.
83. Prince, R. C., S. J. G. Linkletter and P. L. Dutton (1981) The thermodynamic properties of some commonly used oxidation-reduction mediators, inhibitors and dyes, as determined by polarography. Biochim. Biophys. Acta 635, 132-148.
84. Sled', V. D., A. Ja. Mulkidjanian, V. P. Shinkarev, M. I. Verkhovsky and B. S. Kaurov (1984) Direct spectroscopic determination of midpoint-potentials of primary and secondary quinones in the photosynthetic RC's of Rhodospirillum rubrum. Biokhimia (USSR) 49, 204-208.
85. - of photosynthetic reaction centers by an artificial acceptor. FEBS Lett. 197, 263-266.
86. Wraight, C. A. (1979) The role of quinones in bacterial photosynthesis. Photochem. Photobiol. 30, 767-776.
87. - reaction in isolated reaction centers in the photosynthetic bacterium Rhodopseudomonas sphaeroides. Biochim. Biophys. Acta 764, 46-54.
88. Shinkarev, V. P., M. I. Verkhovsky and B. S. Kaurov (1983) Determination of mid-point potential of secondary quinone acceptor in the RCs of Rhodospirillum rubrum cnromatophores. Microbiology (USSR) 16, 271-280.
89. B. Biochim. Biophys. Acta 809, 260-270.
90. Robinson, H. H. and A. R. Crofts (1983) Kinetics of the oxidation-reduction reactions of the photosystem II quinone acceptor complex and the pathway for deactivation. FEBS Lett. 153, 221-226.