Three decades of research in bacterial photosynthesis and the road leading to it: A personal account

Photosynthesis Research

Volumn 55, Issue 1, 1998, Pages 1-40

  Feher, George ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Amino acid titrations; Crystallization; Electron transfer reactions; Electronic structure; Electrostatic calculations; Membrane protein; Proton transfer; Proton coupled electron transfer; Purple bacteria; Reaction center; Reaction center cyt c2 complex; Site directed mutagenesis; Three dimensional structure; X ray crystallography

Indexed keywords

EID: 0031950355     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005985019447     Document Type: Short Survey

References (159)

1. Abramovich S (1992) 'The Best Kept Secret' in Yediot Ahronot, 23 April 1992
2. Abresch EC, Paddock ML, Stowell MHB, McPhillips TM, Axelrod HL, Soltis SM, Rees DC, Okamura MY and Feher G (1998) Identification of proton transfer pathways in the X-ray crystal structure of the bacterial reaction center from Rhodobacter sphaeroides. Photosynth Res (in press)
3. Adir N, Okamura MY and Feher G (1992) Crystallization of the PS II-reaction center. In: Murata N (ed) Research in Photosynthesis, pp II.5.195-II.5.198. Kluwer Academic Publishers, Dordrecht, the Netherlands
4. Adir N, Gilon T, Nechushtai R, Abresch E, Okamura MY and Feher G (1994) Crystallization and X-ray diffraction to 2.9 Å resolution of the reaction center complex of Photosystem II from the thermophilic cyanobacterium Mastigocladus laminosus. Biophys J (Abstracts) 66: A228
5. 2 complex from Rhodobacter sphaeroides. Biochemistry 35: 2535-2547
6. Allen JP, Feher G, Yeates TO, Rees DC, Deisenhofer J, Michel H and Huber R (1986) Structural homology of reaction centers of R. sphaeroides and R. viridis as determined by X-ray diffraction. Proc Natl Acad Sci USA 83: 8589-8593
7. Allen JP, Feher G, Yeates TO, Komiya H and Rees DC (1987) Structure of the reaction center from Rhodobacter sphaeroides R-26 II. The protein subunits. Proc Natl Acad Sci USA 84: 6162-6166
8. Allen JP, Williams JC, Graige M, Paddock ML, Labahn A, Feher G and Okamura MY (1998) Free energy dependence of the direct charge recombination from the primary and secondary quinones in reaction centers from Rhodobacter sphaeroides. Photosynth Res (in press)
9. 2 from Rhodobacter sphaeroides in three crystal forms. Acta Crystallog D50: 596-602
10. a's of ionizable groups in proteins: atomic detail from a continuum electrostatic model. Biochemistry 29: 10219-10225
11. Bennet JE, Ingram DJE, George P and Griffith JS (1955) Paramagnetic resonance absorption of ferrihaemoglobin and ferrimyoglobin derivatives. Nature (London) 176: 394
12. Beroza P, Fredkin DR, Okamura MY and Feher G (1991) Protonation of interacting residues in a protein by a Monte Carlo method: Application to lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides. Proc Natl Acad Sci USA 88: 5804-5808
13. Beroza P, Fredkin DR, Okamura MY and Feher G (1992) Proton transfer pathways in the reaction center of Rhodobacter sphaeroides: A computational study. In: Breton J and Vermeglio A (eds) The Photosynthetic Bacterial Reaction Center II, pp 363-374. Plenum Press, New York
14. Beroza P, Fredkin DR, Okamura MY and Feher G (1995) Electrostatic calculations of amino acid titration and electron transfer. Biophys J 68: 2233-2250
15. Bolton JR, Clayton RK and Reed DN (1969) An identification of the radical giving rise to the light-induced electron spin resonance signal in photosynthetic bacteria. Photochem Photobiol 9: 209-218
16. Boso B, Debrunner P, Okamura MY and Feher G (1981) Mossbauer spectroscopy studies of photosynthetic reaction centers from Rhodopseudomonas sphaeroidesR-26. Biochim Biophys Acta 638: 173-177
17. Bunker G, Stern EA, Blankenship RE and Parson WW (1982) An X-ray absorption study of the iron site in bacterial photosynthetic reaction centers; Biophys J 37: 539-551
18. 2+ in reaction centers from Rhodopseudomonas sphaeroides I. Static magnetization measurements. Biophys J 32: 967-992
19. 2+ in reaction centers from Rhodopseudomonas sphaeroides III. EPR measurements of the reduced acceptor complex. Biophys J 45: 947-973
20. -. Biophys J 58: 149-165
21. Chang CH, Tiede D, Tang J, Smith U, Norris J and Schiffer M (1986) Structure of Rhodopseudomonas sphaeroides R-26 reaction center. FEBS Lett 205: 82-86
22. Chirino AJ, Lous EJ, Huber M, Allen JP, Schenck CC, Paddock ML, Feher G and Rees DC (1994) Crystallographic analyses of site-directed mutants of the photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry 33: 4584-4593
23. Clark WG and Feher G (1963) Nuclear polarization in InSb by a d.c. current. Phys Rev Lett 10: 134-138
24. Clayton RK (1988) Memories of many lives. Photosynth Res 19: 205-224
25. Clayton RK and Wang RT (1971) Photochemical reaction centers from Rhodopseudomonas sphaeroides. Methods Enzymol 23: 696-704
26. Cogdell RJ, Brune DC and Clayton RK (1974) Effects of extraction and replacement of ubiquinone upon the photochemical activity of reaction centers and chromatophores from Rhodopseudomonas sphaeroides. FEBS Lett 45: 344-347
27. Commoner B, Townsend J and Pake GE (1954) Free radicals in biological materials. Nature (London) 174: 689-691
28. DeVault D (1984) Quantum-Mechanical Tunnelling in Biological Systems. Cambridge University Press, Cambridge, UK
29. Debus RJ, Valkirs GE, Okamura MY and Feher G (1982) Localization of the secondary quinone binding site in reaction centers from Rhodopseudomonas sphaeroides R-26 by antibody inhibition of electron transfer. Biochim Biophys Acta 682: 500-503
30. 2+. Biochemistry 25: 2276-2287
31. Deisenhofer J and Michel H (1991) Structures of bacterial photosynthetic reaction centers. Ann Rev Cell Biol 7: 1-23
32. Deisenhofer J, Epp O, Miki K, Huber R and Michel H (1984) X-ray structure analysis of a membrane protein complex: electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J Mol Biol 180: 385-398
33. 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 Å resolution. Nature 318: 618-624
34. 2 and the photosynthetic reaction center of Rhodobacter sphaeroides. Biochemistry 36: 1418-1427
35. Durbin SD and Feher G (1986) Crystal growth studies of lysozyme as a model for protein crystallization. J Crystal Growth 76: 583-592
36. Duysens LNM (1952) Transfer of excitation energy in photosynthesis. Doctoral thesis, Leiden University, the Netherlands
37. 2+ in reaction centers from Rhodopseudomonas sphaeroides II. Extended X-ray fine structure studies. Biophys J 37: 523-538
38. Ermler U, Fritzsch G, Buchanan SK and Michel H (1994) Structure of the photosynthetic reaction center from Rhodobacter sphaeroides at 2.65 Å resolution: Cofactors and protein-cofactor interactions. Structure 2: 925-936
39. Fajer J, Brune DC, Davis MS, Forman A and Spaulding LD (1975) Primary charge separation in bacterial photosynthesis: oxidized chlorophylls and reduced pheophytin. Proc Natl Acad Sci USA 72: 4956-4960
40. Feher G (1959) Electron spin resonance experiments on donors in silicon. I. Electronic structure of donors by the electron nuclear double resonance technique. Phys Rev 114: 1219-1244
41. Feher G (1971) Some chemical and physical properties of a bacterial reaction center particle and its primary photochemical reactants. Photochem Photobiol 14: 373-388
42. Feher G (1988) Light reflections. In: Breton J and Vermeglio A (eds) The Photosynthetic Bacterial Reaction Center, pp 435-440. Plenum Press, New York
43. Feher G (1992) Identification and characterization of the primary donor in bacterial photosynthesis: A chronological account of an EPR/ENDOR investigation. J Chem Soc (Perkin Trans) 2: 1861-1874
44. Feher G (1998a) The development of ENDOR and other reminiscences of the 1950's. In: Eaton G, Eaton S and Sakikhov (eds) Foundations of Modern EPR World Scientific Publishers, River Edge, NJ
45. Feher G (1998b) Light reflections III. Photosynthesis Research (in press)
46. Feher G and Okamura MY (1984) Structure and function of the reaction centers from Rhodopseudomonas sphaeroides. In: Sybesma C (ed) Advances in Photosynthesis Research, Vol II, pp 155-164. M. Nijhoff/Dr. W. Junk, Hingham, MA
47. Feher G and Scovil HED (1957) Electron spin relaxation times in gadolinium ethyl sulfate. Phys Rev 105: 760-762
48. Feher G and Weissman M (1973) Fluctuation spectroscopy: determination of chemical reaction kinetics from the frequency spectrum of fluctuations. Proc Natl Acad Sci USA 70: 870-875
49. Feher G, Prepost R and Sachs AM (1960) Muonium formation in semiconductors. Phys Rev Lett 5: 515-517
50. Feher G, Shepherd W and Shore HB (1966) Paraelectric resonance of OH- dipoles in KCL. Phys Rev Lett 16: 500-503
51. Feher G, Isaacson RA and McElroy JD (1969) Observation of EPR lines using temperature modulation. Rev Sci Instr 40: 1640-1641
52. Feher G, Okamura MY, Rayond JA and Steiner LA (1971) Subunit structure of reaction centers from Rhodopseudomonas sphaeroides. Biophys J (Abstracts) 11: 38a
53. Feher G, Okamura MY and McElroy JD (1972) Identification of an electron acceptor in reaction centers of Rhodopseudomonas sphaeroides by EPR spectroscopy. Biochim Biosphys Acta 244: 222-226
54. Feher G, Isaacson RA, Scholes EP and Nagel R (1973) Electron nuclear double resonance (ENDOR) investigation on myoglobin and hemoglobin. Ann NY Acad Sci 222: 86-101
55. Feher G, Hoff AJ, Isaacson RA and Ackerson LC (1975) ENDOR experiments on chlorophyll and bacteriochlorophyll in vitro and in the photosynthetic unit. Ann NY Acad Sci USA 244: 239-259
56. Feher G, Okamura MY and McElroy JD (1982) Identification of an electron acceptor in reaction centers of Rhodopseudomonas sphaeroides by EPR spectroscopy. Biochim Biophys Acta 267: 222-226
57. Feher G, Isaacson RA, Okamura MY and Lubitz W (1985) ENDOR of semiquinones in reaction centers from Rhodopseudomonas sphaeroides. In: Michel-Beyerle ME (ed) Antennas and Reaction Centers of Photosynthetic Bacteria - Structure, Interactions and Dynamics, pp 174-189. Springer-Verlag, Berlin
58. A in reaction centers from Rhodobacter sphaeroides R-26. In: Breton J and Vermeglio A (eds) The Photosynthetic Bacterial Reaction Center, pp 271-287. Plenum Press, New York
59. Feher G, Allen JP, Okamura MY and Rees DC (1989) Primary Processes in Bacterial Photosynthesis: Structure and Function of Reaction Centers. NATURE 339: 111-116
60. Feher G, Paddock ML, Rongey SH and Okamura MY (1992) Proton transfer pathways in photosynthetic reaction centers studied by site-directed mutagenesis. In: Pullman A and Jortner J, Pullman B (eds) Membrane Proteins: Structure, Interactions and Models, pp 481-495. Kluwer Academic Publishers, Dordrecht, the Netherlands
61. Garavito RM and Rosenbush JP (1980) Three-dimensional crystals of an integral membrane protein: An initial X-ray analysis. J Cell Biol 86: 327-329
62. -, is not electron transfer. Biophys J (Abstracts) 70: A10
63. B) reduction in reaction centers of Rb. sphaeroides. J Am Chem Soc 118: 812-816
64. Griffith JS (1956) On the magnetic properties of some haemoglobin complexes. Proc R Soc (London) A235: 23-36
65. Gunner MR and Honig BH (1992) Calculations of proton uptake in the Rhodobacter sphaeroides reaction centers. In: Breton J and Vermeglio A (eds) The Photosynthetic Bacterial Reaction Center II, pp 403-410. Plenum Press, New York
66. A site and the oxidized bacteriochlorophyll dimer. J Phys Chem 90: 3783-3795
67. Hopfield JJ (1974) Electron transfer between biological molecules by thermally activated tunneling. Proc Natl Acad Sci USA 71: 3640-3644
68. Huber M, Isaacson RA, Abresch EC, Gaul D, Schenck CC and Feher G (1996) Electronic structure of the oxidized electron donor of the HL (M202) and HL (L173) heterodimer mutants of the photosynthetic bacterium Rhodobacter sphaeroides: ENDOR on single crystals of reaction centers. Biochim Biophys Acta 1273: 108-128
69. - in single crystals of reaction centers from Rb. sphaeroides. Biophys J (Abstracts) 68: A246
70. 13C labeled quinones. In: Michel-Beyerle ME (ed) The Reaction Center of Photosynthetic Bacteria - Structure and Dynamics, pp 353-367. Springer-Verlag, Berlin
71. Jortner J (1976) Temperature dependent activation energy for electron transfer between biological molecules. J Chem Phys 64: 4860-4867
72. Kam Z, Shore HB and Feher G (1978) On the crystallization of proteins. J Mol Biol 123: 539-555
73. Kamen MD (1963) Primary Processes in Photosynthesis. Academic Press, New York
74. Kamen MD (1989) Onward with a fabulous half century. Photosynth Res 21: 3-16
75. Katz B (1966) Nerve, Muscle and Synopse. Chapter 9, McGraw Hill, New York
76. -. Biochim Biophys Acta 766: 126-140
77. Kleinfeld D, Okamura MY and Feher G (1984b) Electron transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: Evidence for light induced structural changes. Biochemistry 23: 5780-5786
78. 2-. Biochim Biophys Acta 809: 291-310
79. A site. Chem Phys 197: 355-366
80. Lancaster CRD, Michel H, Honig B and Gunner MR (1996) Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopseudomonas viridis. Biophys J 70: 2469-2492
81. Lendzian F, Huber M, Isaacson RA, Endeward B, Plato M, Bonigk B, Mobius K, Lubitz W and Feher G (1993) The electronic structure of the primary donor cation radical in Rhodobacter sphaeroides R-26: ENDOR and TRIPLE resonance studies in single crystals of reaction centers. Biochim Biophys Acta 1183: 139-160
82. - and associated processes in Rhodobacter R-26 reaction centers. Biochemistry (in press)
83. Lösche M, Feher G and Okamura MY (1987) The stark effect in reaction centers from Rhodobacter sphaeroides R-26 and Rhodopseudomonas viridis. Proc Natl Acad Sci USA 84: 7537-7541
84. Loach PA and Hall RL (1972) The question of the primary electron acceptor in bacterial photosynthesis. Proc Natl Acad Sci USA 69: 786-790
85. Loach PA and Sekura DL (1967) A comparison of decay kinetics of photo-produced absorbance, EPR, and luminescence changes in chromatophores of Rhodospirillum rubrum. Photochem Photobiol 6: 381-393
86. Lous EJ, Huber M, Isaacson RA and Feher G (1990) EPR and ENDOR studies of the oxidized primary donor in single crystals of reaction centers of Rhodobacter sphaeroides R-26. In: Michel-Beyerle ME (ed) Reaction Centers of Photosynthetic Bacteria, pp 45-55. Springer-Verlag, Berlin
87. Lubitz W, Abresch EC, Debus RJ, Isaacson RA, Okamura MY and Feher G (1985) Electron nuclear double resonance of semiquinones in reaction centers of Rhodopseudomonas sphaeroides. Biochim Biophys Acta 808: 464-469
88. Malley M, Feher G and Mauzerall D (1968a) The stark effect in porphyrins. J Mol Spectroscopy 25: 544-548
89. Malley M, Feher G and Mauzerall D (1968b) The zeeman effect in porphyrins. J Mol Spectroscopy 26: 320-334
90. - reaction in isolated reaction centers from the photosynthetic bacterium Rhodopseudomonas sphaeroides. Biochim Biophys Acta 764: 46-54
91. Marcus RA (1993) Electron transfer reactions in chemistry: Theory and experiment (Nobel Lecture) Angewandte Chemie 32: 1111-1222
92. Marinetti TD, Okamura MY and Feher G (1979) Localization of the primary quinone binding site in reaction centers from Rhodopseudomonas sphaeroides R-26 by photoaffinity labeling. Biochemistry 18: 3126-3133
93. + binding by bacterial photosynthetic reaction centers: Comparison of spectrophotometric and conductimetric methods. Biochim Biophys Acta 934: 314-328
94. Mauzerall D and Feher G (1964) A study of the photoinduced porphyrin free radical by electron spin resonance. Biochim Biophys Acta 79: 430-432
95. McElroy D, Feher G and Mauzerall DC (1969) On the nature of the free radical formed during the primary process of bacterial photosynthesis. Biochim Biophys Acta 172: 180-183
96. McElroy JD, Feher G and Mauzerall DC (1972) Characterization of primary reactants in bacterial photosynthesis. I. Comparison of the light-induced EPR signal (g = 2.0026) with that of a bacteriochlorophyll radical. Biochim Biophys Acta 267: 363-374
97. McElroy JD, Mauzerall DC and Feher G (1974) Characterization of primary reactants in bacterial photosynthesis II. Kinetic studies of the light-induced signal (g = 2.0026) and the optical absorbance changes at cryogenic temperatures. Biochim Biophys Acta 333: 261-278
98. -. Biochim Biophys Acta 934: 348-368
99. B leaves the reaction center. Biochim Biophys Acta 1016: 289-292
100. 2 in native and Glu-L212 → Gin mutant reaction centers from Rhodobacter sphaeroides. Biochemistry 33: 1181-1193
101. Michel H and Oesterhelt D (1980) Three-dimensional crystals of membrane proteins: bacteriorhodopsin. Proc Natl Acad Sci USA 77: 1283-1285
102. Michel H (1982) Three-dimensional crystals of a membrane protein complex; the photosynthetic reaction center from Rhodopseudomonas viridis. J Mol Biol 158: 567-572
103. Michel H and Deisenhofer J (1988) Relevance of the photosynthetic reaction center from purple bacteria to the structure of Photosystem II. Biochemistry 27: 1-7
104. Nanba O and Satoh K (1987) Isolation of a Photosystem II reaction center consisting of D-1 and D-2 polypeptides and cytochrome b-5559. Proc Natl Acad Sci USA 84: 109-112
105. Norris JR, Uphaus RA, Crespi HL and Katz JJ (1971) Electron spin resonance of chlorophyll and the origin of signal I in photosynthesis. Proc Natl Acad Sci USA 68: 625-628
106. Norris JR, Scheer H and Katz JJ (1975) Models for antenna and reaction center chlorophylls. Ann NY Acad Sci USA 244: 260-280
107. Okamura MY and Feher G (1986) Isotope effect on electron transfer in reaction centers. Proc Natl Acad Sci USA 83: 8152-8156
108. Okamura MY, Steiner LA and Feher G (1974) Characterization of reaction centers from photosynthetic bacteria. I. Subunit structure of the protein mediating the primary photochemistry in Rhodopseudomonas sphaeroides R-26. Biochem 13: 1394-1403
109. Okamura MY, Isaacson RA and Feher G (1975) The primary acceptor in bacterial photosynthesis: The obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas sphaeroides. Proc Natl Acad Sci USA 72: 3491-3495
110. Okamura MY, Isaacson RA and Feher G (1979a) Spectroscopic and kinetic properties of the transient intermediate acceptor in reaction centers of Rhodopseudomonas sphaeroides. Biochim Biophys Acta 546: 394-417
111. Okamura MY, Fredkin DR, Isaacson RA and Feher G (1979b) Magnetic interactions and electron transfer kinetics of the reduced intermediate acceptor in reaction centers (RCs) of Rhodopseudomonas sphaeroides R-26. Evidence for thermally induced tunneling. In: Chance B, DeVault D, Frauenfelder H, Marcus RA, Schrieffer JR and Sutin N (eds) Biological Systems, pp 729-743. Academic Press, New York
112. Okamura MY, Feher G and Nelson N (1982) Reaction centers. In: Govindjee (ed) Photosynthesis: Energy Conversion by Plants and Bacteria, pp 195-272. Academic Press, New York
113. 2 complex of Photosystem II from spinach: EPR of the triplet state. In: Biggins J (ed) Progress in Photosynthesis Research, Vol 1, pp I.4.379-I.4.381. Martinus Nijhoff, The Hague/Boston/London
114. Paddock ML, Rongey SH, Feher G and Okamura MY (1989) Pathway of proton transfer in bacterial reaction centers: Replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover. Proc Natl Acad Sci USA 86: 6602-6606
115. Paddock ML, McPherson PH, Feher G and Okamura MY (1990) Pathway of proton transfer in bacterial reaction centers: Replacement of serine-L223 by alanine inhibits electron and proton transfers associated with the reduction of quinone to dihydroquinone. Proc Natl Acad Sci USA 87: 6803-6807
116. Paddock, ML, Rongey, SH, McPherson, PH, Juth A, Feher G and Okamura MY (1994) Pathway of proton transfer in bacterial reaction centers: the role of Asp-L213 in proton transfers associated with the reduction of quinone to dihydroquinone. Biochemistry 33: 734-745
117. B by interchanging Asp and Glu at the L212 and L213 sites. Biochemistry 36: 14238-14249
118. - in bacterial reaction centers of Rhodobacter sphaeroides containing the Asp-L2B→Asn lesion Photosynth Res (in press)
119. Page CC, Farid RS, Moser CC and Dutton PL (1996) Modeling electron transfer in redox proteins: A binary tunneling barrier model. Biophys J (Abstracts) 70: A343
120. Parson WW (1968) The role of P870 in bacterial photosynthesis; Biochim Biophys Acta 153: 248-259
121. Parson WW, Clayton RK and Cogdell RJ (1975) Excited states of photosynthetic reaction centers at low redox potential. Biochim Biophys Acta 387: 265-278
122. Peters K, Avouris PH, Rentzepis PM (1978) Picosecond dynamics of primary electron-transfer processes in bacterial photosynthesis. Biophys J 23: 207-217
123. 2 in Rhodopseudomonas sphaeroides and Rhodopseudomonas capsulata. Biochim Biophys Acta 387: 212-227
124. Rautter J, Lendzian F, Schulz C, Fetsch A, Kuhn M, Lin X, Williams JC, Allen JP and Lubitz W (1995) ENDOR studies of the primary donor cation radical in mutant reaction centers of Rhodobacter sphaeroides with altered hydrogen-bond interactions. Biochemistry 34: 8130-8143
125. Reed DW, Clayton RK (1968) Isolation of a reaction center fraction from Rhodopseudomonas sphaeroides. Biochem Biophys Res Commun. 30: 471-475
126. Rongey SH, Paddock ML, Juth AL, McPherson PH, Feher G and Okamura MY (1991) Pathway of proton transfer in bacterial RCs from Rb. sphaeroides: Replacement of Asp-L213 with ASN inhibits electron and proton transfer to the secondary quinone. Biophys J (Abstracts) 59: 142a
127. Rongey SH, Juth AL, Paddock ML, Feher G and Okamura MY (1995) Importance of a carboxylic acid at H173 for proton-coupled electron transfer in RCs of Rb. sphaeroides. Biophys J (Abstracts) 68: A247
128. Rosen D, Okamura MY and Feher G (1980) Interaction of cytochrome c with reaction centers of Rhodopseudomonas sphaeroides R-26. I. Determination of number of binding sites and dissociation constant by equilibrium dialysis. Biochemistry 19: 5687-5692
129. Rosen D, Okamura MY, Abresch EC, Valkirs GE and Feher G (1983) Interaction of cytochrome c with reaction centers of Rhodopseudomonas sphaeroides R-26: localization of the binding site by chemical crosslinking and immunochemical studies. Biochemistry 22: 335-341
130. Schönfeld M, Montai M and Feher G (1979) Functional reconstitution of photosynthetic reaction centers in planar lipid bilayers. Proc Natl Acad Sci USA 76: 6351-6355
131. Schrödinger E (1944) What is Life. Cambridge University Press, Cambridge, UK
132. Scovil HED, Feher G and Seidel H (1957) Operation of a solid state maser. Phys Rev 105: 762-763
133. Sebban P, Maroti P and Hanson DK (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
134. Shepherd I and Feher G (1965) Cooling by adiabatic depolarization of OH- molecules in KCL. Phys Rev Lett 15: 194-198
135. Sogo P, Jost M and Calvin M (1959) Evidence for free-radical production in photosynthesizing systems. Radiation Res (Supplement) 1: 511
136. Steiner LA, Okamura MY, Lopes AD, Moskowitz E and Feher G (1974) Characterization of reaction centers from photosynthetic bacteria. II. Amino acid composition of the reaction center protein and its subunits in Rhodopseudomonas sphaeroides R-26. Biochem 13: 1403-1410
137. Stowell MHB, McPhillips TM, Rees DC, Soltis SM, Abresch E and Feher G (1997) Light induced structural changes and the mechanism of electron/proton transfer in the photosynthetic reaction center. Science 276: 812-816
138. Straley SC, Parson WW, Mauzerall DC and Clayton RK (1973) Pigment content and molar extinction coefficients of photochemical reaction centers from Rhodopseudomonas sphaeroides. Biochim Biophys Acta 305: 597-609
139. Sutton MR, Rosen D, Feher G and Steiner LA (1982) Aminoterminal sequence of L, M and H subunits of RCs from photosynthetic bacterium Rhodopseudomonas sphaeroides R-26. Biochemistry 16: 3842-3849
140. Szent Györgyi A (1957) Bioenergetic. Chapter 6, Academic Press, New York
141. Takahashi E and Wraight CA (1990) A crucial role for AspL213 in the proton transfer pathway to the secondary quinone of reaction centers from Rhodobacter sphaeroides. Biochim Biophys Acta 1020: 107-111
142. B-binding site of Rhodobacter sphaeroides reaction center. FEBS Lett 283: 140-144
143. H173 of the photosynthetic reaction center from Rhodobacter sphaeroides. Biophys J (Abstracts) 68: 95
144. Takahashi E and Wraight CA (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
145. Tiede DM, Prince RC, Reed GH and Dutton PL (1976) EPR properties of the electron carrier intermediate between the reaction center bacteriochlorophylls and the primary acceptor in Chromatium vinosum. FEBS Lett 65: 301-304
146. Tiede DM and Chang CH (1988) The cytochrome-c binding surface of reaction centers from Rhodobacter sphaeroides. Isr J Chem 28: 183-191
147. Trebst A (1987) The three-dimensional structure of the herbicide binding niche on the reaction center polypeptides of Photosystem II. Z. Naturforsch 42c: 742-750
148. Valkirs GE and Feher G (1982) Topography of reaction center in the membrane of the photosynthetic bacterium Rhodopseudomonas sphaeroides. J Cell Biol 95: 179-188
149. Van den Brink JS, Spoyalov AP, Gast P, van Liemt BS, Raap J, Lugtenburg J and Hoff AJ (1994) Asymmetric binding of the primary acceptor quinone in reaction centers of the photosynthetic bacterium sphaeroides R26 probed with Q-band (35 GHz) EPR spectroscopy. FEBS Lett 353: 273-276
150. Weissman M, Schindler H and Feher G (1976) Determination of molecular weights by fluctuation spectroscopy; application to DNA. Proc Natl Acad Sci USA 73: 2776-2780
151. Weissman MB, Isaacson RA and Feher G (1979) Experimental verification of a theory of 1/f noise in a model system. Phys Rev Lett 43: 733-736
152. Williams JC, Steiner LA, Ogden RC, Simon MI and Feher G (1983) Primary structure of the M subunit of the reaction center from Rhodopseudomonas sphaeroides. Proc Natl Acad Sci USA 80: 6505-6509
153. Williams JC, Steiner LA, Feher G and Simon MI (1984) Primary structure of the L subunit of the reaction centers from Rhodopseudomonas sphaeroides. Proc Natl Acad Sci USA 81: 7303-7307
154. Williams JC, Steiner LA and Feher G (1986) Primary structure of the reaction center from Rhodopseudomonas sphaeroides. Proteins 1: 312-325
155. Williams JC, Paddock ML, Feher G and Allen JP (1991) Effects of iron ligand substitutions in reaction centers from Rhodobacter sphaeroides. Biophys J (Abstracts) 59: 142a
156. Woodbury NW and Allen J (1995) The pathway and thermodynamics of electron transfer in wild type and mutant reaction centers of purple non sulfur bacteria. In: Blankenship RE, Madigan MT and Bauer CE (eds) Anoxygenic Photosynthetic Bacteria, pp 527-557. Kluwer Academic Publishers, Dordrecht, the Netherlands.
157. + binding coupled to secondary electron transfer in the quinone acceptor complex. Biochim Biophys Acta 548: 309-327
158. Wraight CA (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
159. Youvan DC, Bylina EJ, Alberti M, Begusch H and Hearst JE (1984) Nucleotide and deduced polypeptide sequence of the photosynthetic reaction center, B870 antenna and flanking polypeptides from Rps. capsulatus. Cell 37: 949-957