| Year |
Citation |
Score |
| 2018 |
Okamura MY, Lubitz W, Allen JP. Remembering George Feher (1924-2017). Photosynthesis Research. PMID 29802563 DOI: 10.1007/S11120-018-0517-9 |
0.362 |
|
| 2013 |
Okamura M. George Feher: a pioneer in reaction center research. Photosynthesis Research. 120: 29-42. PMID 24104959 DOI: 10.1007/S11120-013-9927-X |
0.367 |
|
| 2012 |
Flores M, Okamura MY, Niklas J, Pandelia ME, Lubitz W. Pulse Q-band EPR and ENDOR spectroscopies of the photochemically generated monoprotonated benzosemiquinone radical in frozen alcoholic solution. The Journal of Physical Chemistry. B. 116: 8890-900. PMID 22731760 DOI: 10.1021/Jp304555U |
0.406 |
|
| 2010 |
Flores M, Savitsky A, Paddock ML, Abresch EC, Dubinskii AA, Okamura MY, Lubitz W, Möbius K. Electron-nuclear and electron-electron double resonance spectroscopies show that the primary quinone acceptor QA in reaction centers from photosynthetic bacteria Rhodobacter sphaeroides remains in the same orientation upon light-induced reduction. The Journal of Physical Chemistry. B. 114: 16894-901. PMID 21090818 DOI: 10.1021/Jp107051R |
0.444 |
|
| 2010 |
Paddock ML, Flores M, Isaacson R, Shepherd JN, Okamura MY. EPR and ENDOR Investigation of Rhodosemiquinone in Bacterial Reaction Centers Formed by B-Branch Electron Transfer. Applied Magnetic Resonance. 37: 39. PMID 20157643 DOI: 10.1007/S00723-009-0042-2 |
0.513 |
|
| 2010 |
Flores M, Isaacson R, Shepherd J, Paddock M, Okamura M. Endor Spectrum of the Protonated Rhodosemiquinone in Bacterial Reaction Centers Biophysical Journal. 98: 173a. DOI: 10.1016/J.Bpj.2009.12.935 |
0.36 |
|
| 2009 |
Abresch EC, Gong XM, Paddock ML, Okamura MY. Electron transfer from cytochrome c2 to the reaction center: A transition state model for ionic strength effects due to neutral mutations Biochemistry. 48: 11390-11398. PMID 19877711 DOI: 10.1021/Bi901332T |
0.515 |
|
| 2009 |
Iwata T, Paddock ML, Okamura MY, Kandori H. Identification of FTIR bands due to internal water molecules around the quinone binding sites in the reaction center from rhodobacter sphaeroides Biochemistry. 48: 1220-1229. PMID 19161296 DOI: 10.1021/Bi801990S |
0.427 |
|
| 2009 |
Watanabe A, Iwata T, Paddock ML, Okamura MY, Kandori H. 3TP2-01 FTIR study of metal-replaced bacterial photosynthetic reaction center.(The 47th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 49: S60. DOI: 10.2142/Biophys.49.S60_4 |
0.318 |
|
| 2009 |
Watanabe A, Iwata T, Paddock ML, Okamura MY, Kandori H. 3P-225 FTIR study of metal-replaced bacterial photosynthetic reaction center.(Photobiology:Photosynthesis,Oral Presentations,The 47th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 49: S189. DOI: 10.2142/Biophys.49.S189_1 |
0.31 |
|
| 2009 |
Okamura M, Abresch E, Paddock M. A Neutral Mutation Changes the Ionic Strength Dependence of the Rate of Electron Transfer between Cyt c2 and RCs from Rb. sphaeroides Biophysical Journal. 96: 239a. DOI: 10.1016/J.Bpj.2008.12.1177 |
0.474 |
|
| 2009 |
Lin S, Jaschke P, Wang H, Paddock M, Tufts A, Allen J, Rosell F, Mauk A, Okamura M, Beatty J, Woodbury N. Kinetics and Energetics of Electron Transfer Reactions in a Photosynthetic Bacterial Reaction Center Assembled with Zinc Bacteriochlorophylls Biophysical Journal. 96: 239a. DOI: 10.1016/J.Bpj.2008.12.1175 |
0.485 |
|
| 2009 |
Paddock ML, Abresch EC, Shepherd JN, Okamura MY. Demethyl Ubiquinone Inhibits Catalytic QB Activity In Reaction Centers From Rhodobacter sphaeroides∗ Biophysical Journal. 96: 239a. DOI: 10.1016/J.Bpj.2008.12.1174 |
0.452 |
|
| 2009 |
Flores M, Paddock ML, Abresch EC, Okamura MY, Lubitz W. ENDOR Spectroscopy Shows that QA Remains in the Same Orientation Upon Reduction in Reaction Centers from Rhodobacter Sphaeroides Biophysical Journal. 96: 238a-239a. DOI: 10.1016/J.Bpj.2008.12.1173 |
0.347 |
|
| 2008 |
Abresch EC, Paddock ML, Villalobos M, Chang C, Okamura MY. Interaction between cytochrome c2 and the photosynthetic reaction center from Rhodobacter sphaeroides: Role of interprotein hydrogen bonds in binding and electron transfer Biochemistry. 47: 13318-13325. PMID 19053264 DOI: 10.1021/Bi801675A |
0.434 |
|
| 2008 |
Iwata T, Paddock ML, Okamura MY, Kandori H. 3P-258 Detection of water molecules involved in the proton uptake of a bacterial 2 photosynthetic reaction center(The 46th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 48: S167. DOI: 10.2142/Biophys.48.S167_3 |
0.341 |
|
| 2008 |
Watanabe A, Iwata T, Paddock ML, Okamura MY, Beatty JT, Kandori H. 3P-250 A mutation effect of His-H126/His-H128 on the reduction of Q_A^- in a bacterial reaction center(The 46th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 48: S166. DOI: 10.2142/Biophys.48.S166_1 |
0.365 |
|
| 2007 |
Paddock ML, Isaacson RA, Abresch EC, Okamura MY. Light induced EPR spectra of reaction centers from Rhodobacter sphaeroides at 80K: Evidence for reduction of Q(B) by B-branch electron transfer in native reaction centers. Applied Magnetic Resonance. 31: 29-43. PMID 18163156 DOI: 10.1007/Bf03166246 |
0.467 |
|
| 2007 |
Paddock ML, Flores M, Isaacson R, Chang C, Abresch EC, Okamura MY. ENDOR spectroscopy reveals light induced movement of the H-bond from Ser-L223 upon forming the semiquinone (Q(B)(-)(*)) in reaction centers from Rhodobacter sphaeroides. Biochemistry. 46: 8234-43. PMID 17590017 DOI: 10.1021/bi7005256 |
0.37 |
|
| 2007 |
Nabedryk E, Paddock ML, Okamura MY, Breton J. Monitoring the pH dependence of IR carboxylic acid signals upon Q B - formation in the Glu-L212 → Asp/Asp-L213 → Glu swap mutant reaction center from Rhodobacter sphaeroides Biochemistry. 46: 1176-1182. PMID 17260947 DOI: 10.1021/Bi0619627 |
0.439 |
|
| 2007 |
Iwata T, Paddock ML, Okamura MY, Kandori H. 2P332 Water Molecules around the Secondary Quinone (Q_B) Binding Pockets in the Reaction Center from Rhodobacter sphaeroides(Photobiology-photosynthesis, and vision and photoreception,Oral Presentations) Seibutsu Butsuri. 47: S196. DOI: 10.2142/Biophys.47.S196_1 |
0.387 |
|
| 2007 |
Paddock ML, Isaacson RA, Abresch EC, Okamura MY. Light-induced EPR spectra of reaction centers from Rhodobacter sphaeroides at 80 K: Evidence for reduction of QB by B branch electron transfer in native reaction centers Applied Magnetic Resonance. 31: 29-43. |
0.382 |
|
| 2006 |
Paddock ML, Flores M, Isaacson R, Chang C, Abresch EC, Selvaduray P, Okamura MY. Trapped conformational states of semiquinone (D+*QB-*) formed by B-branch electron transfer at low temperature in Rhodobacter sphaeroides reaction centers. Biochemistry. 45: 14032-42. PMID 17115698 DOI: 10.1021/bi060854h |
0.354 |
|
| 2005 |
Nabedryk E, Paddock ML, Okamura MY, Breton J. An isotope-edited FTIR investigation of the role of Ser-L223 in binding quinone (QB) and semiquinone (QB -) in the reaction center from Rhodobacter sphaeroides Biochemistry. 44: 14519-14527. PMID 16262252 DOI: 10.1021/Bi051328D |
0.438 |
|
| 2005 |
Paddock ML, Weber KH, Chang C, Okamura MY. Interactions between cytochrome c2 and the photosynthetic reaction center from Rhodobacter sphaeroides: The cation-π interaction Biochemistry. 44: 9619-9625. PMID 16008347 DOI: 10.1021/bi050651d |
0.331 |
|
| 2005 |
Axelrod HL, Okamura MY. The structure and function of the cytochrome c2: Reaction center electron transfer complex from Rhodobacter sphaeroides Photosynthesis Research. 85: 101-114. PMID 15977062 DOI: 10.1007/S11120-005-1368-8 |
0.44 |
|
| 2005 |
Paddock ML, Chang C, Xu Q, Abresch EC, Axelrod HL, Feher G, Okamura MY. Quinone (QB) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: quantum efficiency and X-ray structure. Biochemistry. 44: 6920-8. PMID 15865437 DOI: 10.1021/bi047559m |
0.596 |
|
| 2005 |
Miyashita O, Okamura MY, Onuchic JN. Interprotein electron transfer from cytochrome c2 to photosynthetic reaction center: Tunneling across an aqueous interface Proceedings of the National Academy of Sciences of the United States of America. 102: 3558-3563. PMID 15738426 DOI: 10.1073/Pnas.0409600102 |
0.418 |
|
| 2004 |
Miyashita O, Onuchic JN, Okamura MY. Transition state and encounter complex for fast association of cytochrome c2 with bacterial reaction center Proceedings of the National Academy of Sciences of the United States of America. 101: 16174-16179. PMID 15520377 DOI: 10.1073/Pnas.0405745101 |
0.477 |
|
| 2004 |
Nabedryk E, Breton J, Okamura MY, Paddock ML. Identification of a novel protonation pattern for carboxylic acids upon QB photoreduction in Rhodobacter sphaeroides reaction center mutants at Asp-L213 and Glu-L212 sites Biochemistry. 43: 7236-7243. PMID 15182169 DOI: 10.1021/Bi049342Y |
0.449 |
|
| 2004 |
Xu Q, Axelrod HL, Abresch EC, Paddock ML, Okamura MY, Feher G. X-Ray structure determination of three mutants of the bacterial photosynthetic reaction centers from Rb. sphaeroides; altered proton transfer pathways. Structure (London, England : 1993). 12: 703-15. PMID 15062092 DOI: 10.1016/J.Str.2004.03.001 |
0.666 |
|
| 2003 |
Gong XM, Paddock ML, Okamura MY. Interactions between Cytochrome c2 and Photosynthetic Reaction Center from Rhodobacter sphaeroides: Changes in Binding Affinity and Electron Transfer Rate Due to Mutation of Interfacial Hydrophobic Residues Are Strongly Correlated Biochemistry. 42: 14492-14500. PMID 14661961 DOI: 10.1021/Bi035603C |
0.447 |
|
| 2003 |
Paddock ML, Feher G, Okamura MY. Proton transfer pathways and mechanism in bacterial reaction centers. Febs Letters. 555: 45-50. PMID 14630317 DOI: 10.1016/S0014-5793(03)01149-9 |
0.642 |
|
| 2003 |
Miyashita O, Onuchic JN, Okamura MY. Continuum electrostatic model for the binding of cytochrome c2 to the photosynthetic reaction center from Rhodobacter sphaeroides Biochemistry. 42: 11651-11660. PMID 14529275 DOI: 10.1021/Bi0350250 |
0.401 |
|
| 2003 |
Paddock ML, Sagle L, Tehrani A, Beatty JT, Feher G, Okamura MY. Mechanism of proton transfer inhibition by Cd(2+) binding to bacterial reaction centers: determination of the pK(A) of functionally important histidine residues. Biochemistry. 42: 9626-32. PMID 12911304 DOI: 10.1021/bi0346648 |
0.578 |
|
| 2003 |
Miyashita O, Okamura MY, Onuchic JN. Theoretical understanding of the interprotein electron transfer between cytochrome c2 and the photosynthetic reaction center Journal of Physical Chemistry B. 107: 1230-1241. DOI: 10.1021/Jp026753K |
0.449 |
|
| 2002 |
Paddock ML, Adelroth P, Feher G, Okamura MY, Beatty JT. Determination of proton transfer rates by chemical rescue: application to bacterial reaction centers. Biochemistry. 41: 14716-25. PMID 12475220 DOI: 10.1021/bi020419x |
0.628 |
|
| 2002 |
Calvo R, Isaacson RA, Abresch EC, Okamura MY, Feher G. Spin-lattice relaxation of coupled metal-radical spin-dimers in proteins: application to Fe(2+)-cofactor (Q(A)(-.), Q(B)(-.), phi(-.)) dimers in reaction centers from photosynthetic bacteria. Biophysical Journal. 83: 2440-56. PMID 12414679 DOI: 10.1016/S0006-3495(02)75256-9 |
0.552 |
|
| 2002 |
Axelrod HL, Abresch EC, Okamura MY, Yeh AP, Rees DC, Feher G. X-ray structure determination of the cytochrome c2: reaction center electron transfer complex from Rhodobacter sphaeroides. Journal of Molecular Biology. 319: 501-15. PMID 12051924 DOI: 10.1016/S0022-2836(02)00168-7 |
0.61 |
|
| 2002 |
Mezzetti A, Nabedryk E, Breton J, Okamura MY, Paddock ML, Giacometti G, Leibl W. Rapid-scan Fourier transform infrared spectroscopy shows coupling of GLu-L212 protonation and electron transfer to QB in Rhodobacter sphaeroides reaction centers Biochimica Et Biophysica Acta - Bioenergetics. 1553: 320-330. PMID 11997141 DOI: 10.1016/S0005-2728(02)00186-X |
0.501 |
|
| 2002 |
Tetreault M, Cusanovich M, Meyer T, Axelrod H, Okamura MY. Double mutant studies identify electrostatic interactions that are important for docking cytochrome c2 onto the bacterial reaction center Biochemistry. 41: 5807-5815. PMID 11980484 DOI: 10.1021/bi012053e |
0.372 |
|
| 2001 |
Adelroth P, Paddock ML, Tehrani A, Beatty JT, Feher G, Okamura MY. Identification of the proton pathway in bacterial reaction centers: decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors. Biochemistry. 40: 14538-46. PMID 11724567 DOI: 10.1021/bi011585s |
0.637 |
|
| 2001 |
Nabedryk E, Breton J, Okamura MY, Paddock ML. Simultaneous replacement of Asp-L210 and Asp-M17 with Asn increases proton uptake by Glu-L212 upon first electron transfer to QB in reaction centers from Rhodobacter sphaeroides Biochemistry. 40: 13826-13832. PMID 11705371 DOI: 10.1021/Bi011423W |
0.49 |
|
| 2001 |
Tetreault M, Rongey SH, Feher G, Okamura MY. Interaction between cytochrome c2 and the photosynthetic reaction center from Rhodobacter sphaeroides: effects of charge-modifying mutations on binding and electron transfer. Biochemistry. 40: 8452-62. PMID 11456482 DOI: 10.1021/bi010222p |
0.572 |
|
| 2001 |
Paddock ML, Adelroth P, Chang C, Abresch EC, Feher G, Okamura MY. Identification of the proton pathway in bacterial reaction centers: cooperation between Asp-M17 and Asp-L210 facilitates proton transfer to the secondary quinone (QB). Biochemistry. 40: 6893-902. PMID 11389604 DOI: 10.1021/bi010280a |
0.644 |
|
| 2001 |
Calvo R, Isaacson RA, Paddock ML, Abresch EC, Okamura MY, Maniero AL, Brunel LC, Feher G. EPR study of the semiquinone biradical QA ̇-QB ̇- in photosynthetic reaction centers of Rhodobacter sphaeroides at 326 GHz: Determination of the exchange interaction Jo Journal of Physical Chemistry B. 105: 4053-4057. DOI: 10.1021/Jp0102670 |
0.593 |
|
| 2000 |
Adelroth P, Paddock ML, Sagle LB, Feher G, Okamura MY. Identification of the proton pathway in bacterial reaction centers: both protons associated with reduction of QB to QBH2 share a common entry point. Proceedings of the National Academy of Sciences of the United States of America. 97: 13086-91. PMID 11078513 DOI: 10.1073/Pnas.230439597 |
0.667 |
|
| 2000 |
Okamura MY, Paddock ML, Graige MS, Feher G. Proton and electron transfer in bacterial reaction centers. Biochimica Et Biophysica Acta. 1458: 148-63. PMID 10812030 DOI: 10.1016/S0005-2728(00)00065-7 |
0.682 |
|
| 2000 |
Paddock ML, Feher G, Okamura MY. Identification of the proton pathway in bacterial reaction centers: replacement of Asp-M17 and Asp-L210 with asn reduces the proton transfer rate in the presence of Cd2+. Proceedings of the National Academy of Sciences of the United States of America. 97: 1548-53. PMID 10677498 DOI: 10.1073/pnas.97.4.1548 |
0.608 |
|
| 2000 |
Axelrod HL, Abresch EC, Paddock ML, Okamura MY, Feher G. Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers. Proceedings of the National Academy of Sciences of the United States of America. 97: 1542-7. PMID 10677497 DOI: 10.1073/pnas.97.4.1542 |
0.561 |
|
| 2000 |
Calvo R, Abresch EC, Bittl R, Feher G, Hofbauer W, Isaacson RA, Lubitz W, Okamura MY, Paddock ML. EPR study of the molecular and electronic structure of the semiquinone biradical Q(A)-(·)Q(B)-(·) in photosynthetic reaction centers from Rhodobacter sphaeroides Journal of the American Chemical Society. 122: 7327-7341. DOI: 10.1021/ja000399r |
0.578 |
|
| 1999 |
Graige MS, Paddock ML, Feher G, Okamura MY. Observation of the protonated semiquinone intermediate in isolated reaction centers from Rhodobacter sphaeroides: implications for the mechanism of electron and proton transfer in proteins. Biochemistry. 38: 11465-73. PMID 10471298 DOI: 10.1021/bi990708u |
0.625 |
|
| 1999 |
Paddock ML, Graige MS, Feher G, Okamura MY. Identification of the proton pathway in bacterial reaction centers: inhibition of proton transfer by binding of Zn2+ or Cd2+. Proceedings of the National Academy of Sciences of the United States of America. 96: 6183-8. PMID 10339562 DOI: 10.1073/pnas.96.11.6183 |
0.617 |
|
| 1998 |
Nabedryk E, Breton J, Okamura MY, Paddock ML. Proton uptake by carboxylic acid groups upon photoreduction of the secondary quinone (Q(B)) in bacterial reaction centers from Rhodobacter sphaeroides: FTIR studies on the effects of replacing Glu H173 Biochemistry. 37: 14457-14462. PMID 9772172 DOI: 10.1021/Bi981139D |
0.436 |
|
| 1998 |
Graige MS, Feher G, Okamura MY. Conformational gating of the electron transfer reaction QA-.QB --> QAQB-. in bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay. Proceedings of the National Academy of Sciences of the United States of America. 95: 11679-84. PMID 9751725 DOI: 10.1073/pnas.95.20.11679 |
0.63 |
|
| 1998 |
Abresch EG, Paddock ML, Stowell MHB, McPhillips TM, Axelrod HL, Soltis SM, Rees DC, Okamura MY, Feher G. Identification of proton transfer pathways in the x-ray crystal structure of the bacterial reaction center from Rhodobacter sphaeroides Photosynthesis Research. 55: 119-125. DOI: 10.1023/A:1006047519260 |
0.623 |
|
| 1998 |
Chen XY, Yurkov V, Paddock ML, Okamura MY, Beatty JT. A puhA gene deletion and plasmid complementation system for facile site directed mutagenesis studies of the reaction center H protein of Rhodobacter sphaeroides Photosynthesis Research. 55: 369-373. DOI: 10.1023/A:1005983903558 |
0.307 |
|
| 1998 |
Allen JP, Williams JC, Graige MS, Paddock ML, Labahn A, Feher G, Okamura MY. Free energy dependence of the direct charge recombination from the primary and secondary quinones in reaction centers from Rhodobacter sphaeroides Photosynthesis Research. 55: 227-233. DOI: 10.1023/A:1005977901937 |
0.628 |
|
| 1998 |
Nabedryk E, Breton J, Okamura MY, Paddock ML. Direct evidence of structural changes in reaction centers of Rb. sphaeroides containing suppressor mutations for Asp L213 → Asn: A FTIR study of Q(B) photoreduction Photosynthesis Research. 55: 293-299. DOI: 10.1023/A:1005969700120 |
0.439 |
|
| 1998 |
Paddock ML, Senft ME, Graige MS, Rongey SH, Turanchik T, Feher G, Okamura MY. Characterization of second site mutations show that fast proton transfer to Q(B)- is restored in bacterial reaction centers of Rhodobacter sphaeroides containing the Asp-L213 → Asn lesion Photosynthesis Research. 55: 281-291. DOI: 10.1023/A:1005953615604 |
0.678 |
|
| 1998 |
Feher G, Okamura MY. The primary and secondary acceptors in bacterial photosynthesis: II. The structure of the Fe2+-Q- complex Applied Magnetic Resonance. 16: 63-100. DOI: 10.1007/Bf03161915 |
0.593 |
|
| 1997 |
Paddock ML, Feher G, Okamura MY. Proton and electron transfer to the secondary quinone (QB) in bacterial reaction centers: the effect of changing the electrostatics in the vicinity of QB by interchanging asp and glu at the L212 and L213 sites. Biochemistry. 36: 14238-49. PMID 9369497 DOI: 10.1021/bi971192m |
0.625 |
|
| 1997 |
Brzezinski P, Paddock ML, Okamura MY, Feher G. Light-induced electrogenic events associated with proton uptake upon forming QB- in bacterial wild-type and mutant reaction centers. Biochimica Et Biophysica Acta. 1321: 149-56. PMID 9332502 DOI: 10.1016/S0005-2728(97)00052-2 |
0.599 |
|
| 1996 |
Adir N, Axelrod HL, Beroza P, Isaacson RA, Rongey SH, Okamura MY, Feher G. Co-crystallization and characterization of the photosynthetic reaction center-cytochrome c2 complex from Rhodobacter sphaeroides. Biochemistry. 35: 2535-47. PMID 8611557 DOI: 10.1021/bi9522054 |
0.519 |
|
| 1996 |
Graige MS, Paddock ML, Bruce JM, Feher G, Okamura MY. Mechanism of proton-coupled electron transfer for quinone (Q(B) reduction in reaction centers of Rb. Sphaeroides Journal of the American Chemical Society. 118: 9005-9016. DOI: 10.1021/ja960056m |
0.636 |
|
| 1995 |
Hienerwadel R, Grzybek S, Fogel C, Kreutz W, Okamura MY, Paddock ML, Breton J, Nabedryk E, Mäntele W. Protonation of Glu L212 following QB - formation in the photosynthetic reaction center of Rhodobacter sphaeroides: Evidence from time-resolved infrared spectroscopy Biochemistry. 34: 2832-2843. PMID 7893696 |
0.345 |
|
| 1995 |
Beroza P, Fredkin DR, Okamura MY, Feher G. Electrostatic calculations of amino acid titration and electron transfer, Q-AQB-->QAQ-B, in the reaction center. Biophysical Journal. 68: 2233-50. PMID 7647231 DOI: 10.1016/S0006-3495(95)80406-6 |
0.656 |
|
| 1995 |
Paddock ML, Feher G, Okamura MY. Pathway of proton transfer in bacterial reaction centers: further investigations on the role of Ser-L223 studied by site-directed mutagenesis. Biochemistry. 34: 15742-50. PMID 7495805 DOI: 10.1021/bi00048a019 |
0.614 |
|
| 1995 |
Labahn A, Bruce JM, Okamura MY, Feher G. Direct charge recombination from D+QAQB - to DQAQB in bacterial reaction centers from Rhodobacter sphaeroides containing low potential quinone in the QA site Chemical Physics. 197: 355-366. DOI: 10.1016/0301-0104(95)00165-K |
0.592 |
|
| 1994 |
Paddock ML, Rongey SH, McPherson PH, Juth A, Feher G, Okamura MY. Pathway of proton transfer in bacterial reaction centers: role of aspartate-L213 in proton transfers associated with reduction of quinoneto dihydroquinone. Biochemistry. 33: 734-45. PMID 8292601 |
0.611 |
|
| 1994 |
McPherson PH, Schönfeld M, Paddock ML, Okamura MY, Feher G. Protonation and free energy changes associated with formation of QBH2 in native and Glu-L212-->Gln mutant reaction centers from Rhodobacter sphaeroides. Biochemistry. 33: 1181-93. PMID 8110749 |
0.615 |
|
| 1994 |
Labahn A, Paddock ML, McPherson PH, Okamura MY, Feher G. Direct Charge Recombination from D+QAQB- to DQAQB in Bacterial Reaction Centers from Rhodobacter sphaeroides The Journal of Physical Chemistry. 98: 3417-3423. DOI: 10.1021/J100064A024 |
0.587 |
|
| 1993 |
McPherson PH, Okamura MY, Feher G. Light-induced proton uptake by photosynthetic reaction centers from Rhodobacter sphaeroides R-26.1. II. Protonation of the state DQAQB2-. Biochimica Et Biophysica Acta. 1144: 309-24. PMID 8399281 DOI: 10.1016/0005-2728(93)90116-W |
0.635 |
|
| 1993 |
Rongey SH, Paddock ML, Feher G, Okamura MY. 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. Proceedings of the National Academy of Sciences of the United States of America. 90: 1325-9. PMID 8381964 DOI: 10.1073/Pnas.90.4.1325 |
0.678 |
|
| 1992 |
Okamura MY, Feher G. Proton transfer in reaction centers from photosynthetic bacteria. Annual Review of Biochemistry. 61: 861-96. PMID 1323240 DOI: 10.1146/annurev.bi.61.070192.004241 |
0.607 |
|
| 1991 |
Paddock ML, Feher G, Okamura MY. Reaction centers from three herbicide resistant mutants of Rhodobacter sphaeroides 2.4.1: Kinetics of electron transfer reactions. Photosynthesis Research. 27: 109-19. PMID 24414574 DOI: 10.1007/BF00033250 |
0.558 |
|
| 1991 |
Beroza P, Fredkin DR, Okamura MY, Feher G. Protonation of interacting residues in a protein by a Monte Carlo method: application to lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides. Proceedings of the National Academy of Sciences of the United States of America. 88: 5804-8. PMID 2062860 DOI: 10.1073/Pnas.88.13.5804 |
0.583 |
|
| 1990 |
Paddock ML, McPherson PH, Feher G, Okamura MY. Pathway of proton transfer in bacterial reaction centers: replacement of serine-L223 by alanine inhibits electron and proton transfers associated with reduction of quinone to dihydroquinone. Proceedings of the National Academy of Sciences of the United States of America. 87: 6803-7. PMID 2168561 |
0.64 |
|
| 1990 |
Calvo R, Passeggi MC, Isaacson RA, Okamura MY, Feher G. Electron paramagnetic resonance investigation of photosynthetic reaction centers from Rhodobacter sphaeroides R-26 in which Fe2+ was replaced by Cu2+. Determination of hyperfine interactions and exchange and dipole-dipole interactions between Cu2+ and QA-. Biophysical Journal. 58: 149-65. PMID 2166597 DOI: 10.1016/S0006-3495(90)82361-4 |
0.518 |
|
| 1990 |
McPherson PH, Nagarajan V, Parson WW, Okamura MY, Feher G. pH-dependence of the free energy gap between DQA and D+Q- A determined from delayed fluorescence in reaction centers from Rhodobacter sphaeroides R-26 Bba - Bioenergetics. 1019: 91-94. DOI: 10.1016/0005-2728(90)90128-Q |
0.61 |
|
| 1990 |
McPherson PH, Okamura MY, Feher G. Electron transfer from the reaction center of Rb. sphaeroides to the quinone pool: Doubly reduced QB leaves the reaction center Bba - Bioenergetics. 1016: 289-292. DOI: 10.1016/0005-2728(90)90071-B |
0.677 |
|
| 1989 |
Paddock ML, Rongey SH, Feher G, Okamura MY. Pathway of proton transfer in bacterial reaction centers: replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover. Proceedings of the National Academy of Sciences of the United States of America. 86: 6602-6. PMID 2570421 DOI: 10.1073/Pnas.86.17.6602 |
0.685 |
|
| 1989 |
Long JE, Durham B, Okamura M, Millett F. Role of specific lysine residues in binding cytochrome c2 to the Rhodobacter sphaeroides reaction center in optimal orientation for rapid electron transfer. Biochemistry. 28: 6970-4. PMID 2554961 DOI: 10.1021/Bi00443A029 |
0.419 |
|
| 1989 |
Lubitz W, Isaacson RA, Okamura MY, Abresch EC, Plato M, Feher G. ENDOR studies of the intermediate electron acceptor radical anion I-. in Photosystem II reaction centers. Biochimica Et Biophysica Acta. 977: 227-32. PMID 2553112 DOI: 10.1016/S0005-2728(89)80076-3 |
0.616 |
|
| 1989 |
Feher G, Allen JP, Okamura MY, Rees DC. Structure and function of bacterial photosynthetic reaction centres Nature. 339: 111-116. DOI: 10.1038/339111A0 |
0.624 |
|
| 1988 |
Paddock ML, Rongey SH, Abresch EC, Feher G, Okamura MY. Reaction centers from three herbicide-resistant mutants of Rhodobacter sphaeroides 2.4.1: sequence analysis and preliminary characterization. Photosynthesis Research. 17: 75-96. PMID 24429662 DOI: 10.1007/Bf00047682 |
0.598 |
|
| 1988 |
McPherson PH, Okamura MY, Feher G. Light-induced proton uptake by photosynthetic reaction centers from Rhodobacter sphaeroides R-26. I. Protonation of the one-electron states D+QA -, DQA -, D+QAQB -, and DQAQB - Bba - Bioenergetics. 934: 348-368. DOI: 10.1016/0005-2728(88)90093-X |
0.629 |
|
| 1987 |
Lösche M, Feher G, Okamura MY. The Stark effect in reaction centers from Rhodobacter sphaeroides R-26 and Rhodopseudomonas viridis. Proceedings of the National Academy of Sciences of the United States of America. 84: 7537-41. PMID 3313396 DOI: 10.1073/Pnas.84.21.7537 |
0.501 |
|
| 1987 |
Hall J, Zha XH, Durham B, O'Brien P, Vieira B, Davis D, Okamura M, Millett F. Reaction of cytochromes c and c2 with the Rhodobacter sphaeroides reaction center involves the heme crevice domain. Biochemistry. 26: 4494-500. PMID 2822094 DOI: 10.1021/Bi00388A048 |
0.422 |
|
| 1986 |
Okamura MY, Feher G. Isotope effect on electron transfer in reaction centers from Rhodopseudomonas sphaeroides. Proceedings of the National Academy of Sciences of the United States of America. 83: 8152-6. PMID 16593776 DOI: 10.1073/Pnas.83.21.8152 |
0.679 |
|
| 1986 |
Kirmaier C, Holten D, Debus RJ, Feher G, Okamura MY. Primary photochemistry of iron-depleted and zinc-reconstituted reaction centers from Rhodopseudomonas sphaeroides. Proceedings of the National Academy of Sciences of the United States of America. 83: 6407-11. PMID 16593750 DOI: 10.1073/Pnas.83.17.6407 |
0.625 |
|
| 1986 |
Debus RJ, Feher G, Okamura MY. Iron-depleted reaction centers from Rhodopseudomonas sphaeroides R-26.1: characterization and reconstitution with Fe2+, Mn2+, Co2+, Ni2+, Cu2+, and Zn2+. Biochemistry. 25: 2276-87. PMID 3011083 DOI: 10.1021/Bi00356A064 |
0.599 |
|
| 1986 |
Okamura MY, Feher G. Isotope effect on electron transfer in reaction centers from Rhodopseudomonas sphaeroides Proceedings of the National Academy of Sciences of the United States of America. 83: 8152-8156. |
0.61 |
|
| 1985 |
Kleinfeld D, Okamura MY, Fcher G. Electron transfer in reaction centers of Rhodopseudomonas sphaeroides. II. Free energy and kinetic relations between the acceptor states Q(-)A Q(-)B and QAQ(2-)B. Biochimica Et Biophysica Acta. 809: 291-310. PMID 21780325 DOI: 10.1016/0005-2728(85)90179-3 |
0.537 |
|
| 1985 |
Kleinfeld D, Okamura MY, Feher G. Charge recombination kinetics as a probe of protonation of the primary acceptor in photosynthetic reaction centers. Biophysical Journal. 48: 849-52. PMID 3907729 DOI: 10.1016/S0006-3495(85)83844-3 |
0.595 |
|
| 1985 |
Gopher A, Blatt Y, Schönfeld M, Okamura MY, Feher G, Montal M. The effect of an applied electric field on the charge recombination kinetics in reaction centers reconstituted in planar lipid bilayers. Biophysical Journal. 48: 311-20. PMID 3902109 DOI: 10.1016/S0006-3495(85)83784-X |
0.594 |
|
| 1985 |
Lubitz W, Abresch EC, Debus RJ, Isaacson RA, Okamura MY, Feher G. Electron nuclear double resonance of semiquinones in reaction centers of Rhodopseudomonas sphaeroides. Biochimica Et Biophysica Acta. 808: 464-9. PMID 2990555 DOI: 10.1016/0005-2728(85)90155-0 |
0.629 |
|
| 1985 |
Debus RJ, Feher G, Okamura MY. LM complex of reaction centers from rhodopseudomonas sphaeroides R-26: Characterization and reconstitution with the H subunit Biochemistry. 24: 2488-2500. DOI: 10.1021/Bi00331A015 |
0.561 |
|
| 1985 |
Okamura MY, Abresch EC, Debus RJ. Reaction centers from triazine-resistant strains of Rhodopseudomonas sphaeroides: Localization of the mutation site by protein hybridization experiments Bba - Bioenergetics. 810: 110-113. DOI: 10.1016/0005-2728(85)90211-7 |
0.395 |
|
| 1985 |
Kleinfeld D, Okamura MY, Feher G. Electron transfer in reaction centers of Rhodopseudomonas sphaeroides. II. Free energy and kinetic relations between the acceptor states QA -QB - and QAQ2- B Bba - Bioenergetics. 809: 291-310. DOI: 10.1016/0005-2728(85)90179-3 |
0.587 |
|
| 1984 |
Kleinfeld D, Abresch EC, Okamura MY, Feher G. Damping of oscillations in the semiquinone absorption in reaction centers after successive flashes determination of the equilibrium between Q(-)AQB and QAQ(-)B. Biochimica Et Biophysica Acta. 765: 406-9. PMID 21780326 DOI: 10.1016/0005-2728(84)90183-X |
0.575 |
|
| 1984 |
Kleinfeld D, Okamura MY, Feher G. Electron-transfer kinetics in photosynthetic reaction centers cooled to cryogenic temperatures in the charge-separated state: evidence for light-induced structural changes. Biochemistry. 23: 5780-6. PMID 6395882 DOI: 10.1021/Bi00319A017 |
0.579 |
|
| 1984 |
Kleinfeld D, Okamura MY, Feher G. Electron transfer in reaction centers of Rhodopseudomonas sphaeroides. I. Determination of the charge recombination pathway of D+QAQ(-)B and free energy and kinetic relations between Q(-)AQB and QAQ(-)B. Biochimica Et Biophysica Acta. 766: 126-40. PMID 6331502 DOI: 10.1016/0005-2728(84)90224-X |
0.669 |
|
| 1984 |
Butler WF, Calvo R, Fredkin DR, Isaacson RA, Okamura MY, Feher G. The electronic structure of Fe2+ in reaction centers from Rhodopseudomonas sphaeroides. III. EPR measurements of the reduced acceptor complex. Biophysical Journal. 45: 947-973. PMID 6329347 DOI: 10.1016/S0006-3495(84)84241-1 |
0.589 |
|
| 1983 |
Rosen D, Okamura MY, Abresch EC, Valkirs GE, Feher G. Interaction of cytochrome c with reaction centers of Rhodopseudomonas sphaeroides R-26: Localization of the binding site by chemical cross-linking and immunochemical studies Biochemistry. 22: 335-341. PMID 6297545 |
0.561 |
|
| 1982 |
Eisenberger P, Okamura MY, Feher G. The electronic structure of Fe2+ in reaction centers from Rhodopseudomonas sphaeroides. II. Extended x-ray fine structure studies. Biophysical Journal. 37: 523-38. PMID 6977381 DOI: 10.1016/S0006-3495(82)84698-5 |
0.539 |
|
| 1982 |
Debus RJ, Valkirs GE, Okamura MY, Feher G. Localization of the secondary quinone-binding site in reaction centers from Rhodopseudomonas sphaeroides R-26 by antibody inhibition of electron transfer Bba - Bioenergetics. 682: 500-503. DOI: 10.1016/0005-2728(82)90067-6 |
0.644 |
|
| 1981 |
Boso B, Debrunner P, Okamura MY, Feher G. Mössbauer spectroscopy studies of photosynthetic reaction centers from Rhodopseudomonas sphaeroides R-26 Bba - Bioenergetics. 638: 173-177. DOI: 10.1016/0005-2728(81)90200-0 |
0.597 |
|
| 1980 |
Butler WF, Johnston DC, Shore HB, Fredkin DR, Okamura MY, Feher G. The electronic structure of Fe2+ in reaction centers from Rhodopseudomonas sphaeroides. I. Static magnetization measurements. Biophysical Journal. 32: 967-92. PMID 6266540 DOI: 10.1016/S0006-3495(80)85030-2 |
0.586 |
|
| 1980 |
Rosen D, Okamura MY, Feher G. Interaction of cytochrome c with reaction centers of Rhodopseudomonas sphaeroides R-26: Determination of number of binding sites and dissociation constants by equilibrium dialysis Biochemistry. 19: 5687-5692. PMID 6257286 |
0.534 |
|
| 1979 |
Marinetti TD, Okamura MY, Feher G. Localization of the primary quinone binding site in reaction centers from rhodopseudomonas sphaeroides R-26 by photoaffinity labeling Biochemistry. 18: 3126-3133. PMID 223628 |
0.504 |
|
| 1979 |
Okamura MY, Isaacson RA, Feher G. Spectroscopic and kinetic properties of the transient intermediate acceptor in reaction centers of Rhodopseudomonas sphaeroides Bba - Bioenergetics. 546: 394-417. PMID 36906 DOI: 10.1016/0005-2728(79)90076-8 |
0.675 |
|
| 1977 |
Feher G, Okamura MY. Reaction centers from Rhodopseudomonas sphaeroides Brookhaven Symposia in Biology. 183-194. PMID 1088799 |
0.54 |
|
| 1975 |
Okamura MY, Isaacson RA, Feher G. Primary acceptor in bacterial photosynthesis: obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas spheroides Proceedings of the National Academy of Sciences of the United States of America. 72: 3491-3495. PMID 1081231 |
0.593 |
|
| 1974 |
Feher G, Isaacson RA, McElroy JD, Ackerson LC, Okamura MY. On the question of the primary acceptor in bacterial photosynthesis: Manganese substituting for iron in reaction centers of Rhodopseudomonas spheroides R-26 Bba - Bioenergetics. 368: 135-139. PMID 4371037 DOI: 10.1016/0005-2728(74)90104-2 |
0.575 |
|
| 1974 |
Steiner LA, Okamura MY, Lopes AD, Moskowitz E, Feher G. Characterization of reaction centers from photosynthetic bacteria. II. Amino acid composition of the reaction center protein and its subunits in Rhodopseudomonas spheroides R-26. Biochemistry. 13: 1403-10. PMID 4206664 DOI: 10.1021/Bi00704A014 |
0.52 |
|
| 1974 |
Okamura MY, Steiner LA, Feher G. Characterization of reaction centers from photosynthetic bacteria. I. Subunit structure of the protein mediating the primary photochemistry in Rhodopseudomonas spheroides R-26 Biochemistry. 13: 1394-1403. PMID 4132124 DOI: 10.1021/Bi00704A013 |
0.512 |
|
| 1974 |
Steiner LA, Okamura MY, Lopes AD, Moskowitz E, Feher G. Characterization of reaction centers from photosynthetic bacteria. II. Amino acid composition of the reaction center protein and its subunits in Rhodopseudomonas spheroides R-26 Biochemistry. 13: 1403-1410. |
0.52 |
|
| 1972 |
Feher G, Okamura MY, McElroy JD. Identification of an electron acceptor in reaction centers of Rhodopseudomonas spheroides by EPR spectroscopy. Biochimica Et Biophysica Acta. 267: 222-6. PMID 4336313 DOI: 10.1016/0005-2728(72)90155-7 |
0.618 |
|
| 1971 |
Garbett K, Johnson CE, Klotz IM, Okamura MY, Williams RJ. Hemerythrin: further studies of Mössbauer spectra. Archives of Biochemistry and Biophysics. 142: 574-83. PMID 5550160 DOI: 10.1016/0003-9861(71)90521-2 |
0.442 |
|
| 1969 |
Okamura MY, Klotz IM, Johnson CE, Winter MR, Williams RJ. The state of iron in hemerythrin. A Mössbauer study. Biochemistry. 8: 1951-8. PMID 4306639 DOI: 10.1021/Bi00833A027 |
0.39 |
|
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