| scholarly article | Q13442814 |
| P356 | DOI | 10.1016/S0005-2728(97)00052-2 |
| P698 | PubMed publication ID | 9332502 |
| P50 | author | George Feher | Q1507337 |
| P2093 | author name string | M Y Okamura | |
| M L Paddock | |||
| P Brzezinski | |||
| P2860 | cites work | Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 A resolution: cofactors and protein-cofactor interactions | Q27730373 |
| Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer | Q27736266 | ||
| Protonation of interacting residues in a protein by a Monte Carlo method: application to lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides | Q29031745 | ||
| Electrostatic calculations of amino acid titration and electron transfer, Q-AQB-->QAQ-B, in the reaction center | Q30052790 | ||
| Structure of the reaction center from Rhodobacter sphaeroides R-26: protein-cofactor (quinones and Fe2+) interactions | Q33670297 | ||
| Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopseudomonas viridis | Q34017828 | ||
| Light-induced voltage changes associated with electron and proton transfer in photosystem II core complexes reconstituted in phospholipid monolayers | Q34115486 | ||
| The effect of an applied electric field on the charge recombination kinetics in reaction centers reconstituted in planar lipid bilayers | Q34256927 | ||
| Pathway of proton transfer in bacterial reaction centers: replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover | Q34300646 | ||
| Proton transfer in reaction centers from photosynthetic bacteria | Q35231392 | ||
| Protonation of Glu L212 following QB- formation in the photosynthetic reaction center of Rhodobacter sphaeroides: evidence from time-resolved infrared spectroscopy | Q36720125 | ||
| Rhodopsin in model membranes: charge displacements in interfacial layers | Q37598562 | ||
| 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 | Q37669865 | ||
| Electrical demonstration of rapid light-induced conformational changes in bacteriorhodopsin | Q39145864 | ||
| Electron acceptors of bacterial photosynthetic reaction centers II. H+ binding coupled to secondary electron transfer in the quinone acceptor complex | Q39286158 | ||
| Electron and proton transfer to the quinones in bacterial photosynthetic reaction centers: insight from combined approaches of molecular genetics and biophysics | Q40962622 | ||
| Pathway of proton transfer in bacterial reaction centers: role of aspartate-L213 in proton transfers associated with reduction of quinoneto dihydroquinone | Q43411068 | ||
| Protonation and free energy changes associated with formation of QBH2 in native and Glu-L212-->Gln mutant reaction centers from Rhodobacter sphaeroides. | Q46025009 | ||
| Proton and electron transfer in the acceptor quinone complex of Rhodobacter sphaeroides reaction centers: characterization of site-directed mutants of the two ionizable residues, GluL212 and AspL213, in the QB binding site | Q52426958 | ||
| 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 | Q52691379 | ||
| Electrogenesis associated with proton transfer in the reaction center protein of the purple bacterium Rhodobacter sphaeroides | Q58047878 | ||
| Structure and function of bacterial photosynthetic reaction centres | Q59068081 | ||
| Fourier Transform Infrared Difference Spectroscopy of Secondary Quinone Acceptor Photoreduction in Proton Transfer Mutants of Rhodobacter sphaeroides | Q71786408 | ||
| Electrostatic dominoes: long distance propagation of mutational effects in photosynthetic reaction centers of Rhodobacter capsulatus | Q71840950 | ||
| Distant electrostatic interactions modulate the free energy level of QA- in the photosynthetic reaction center | Q71853421 | ||
| P433 | issue | 2 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 149-156 | |
| P577 | publication date | 1997-08-01 | |
| P1433 | published in | Biochimica et Biophysica Acta | Q864239 |
| P1476 | title | Light-induced electrogenic events associated with proton uptake upon forming QB- in bacterial wild-type and mutant reaction centers | |
| P478 | volume | 1321 |
| Q30870764 | Biophysical aspects of intra-protein proton transfer |
| Q43647823 | Electrogenic proton transfer in Rhodobacter sphaeroides reaction centers: effect of coenzyme Q(10) substitution by decylubiquinone in the Q(B) binding site |
| Q77360111 | Flash-induced changes in buffering capacity of reaction centers from photosynthetic bacteria reveal complex interaction between quinone pockets |
| Q73378081 | Fusion of chromatophores from photosynthetic bacteria with a supported lipid layer: characterization of the electric units |
| Q34067300 | Key role of proline L209 in connecting the distant quinone pockets in the reaction center of Rhodobacter sphaeroides |
| Q34025599 | Modeling gating charge and voltage changes in response to charge separation in membrane proteins |
| Q40179275 | Photosynthetic electron transfer controlled by protein relaxation: analysis by Langevin stochastic approach |
| Q33919268 | Proton and electron transfer in bacterial reaction centers |
| Q43984323 | Rapid-scan Fourier transform infrared spectroscopy shows coupling of GLu-L212 protonation and electron transfer to Q(B) in Rhodobacter sphaeroides reaction centers |
| Q44583881 | Redox potential of quinones in both electron transfer branches of photosystem I. |
| Q58047773 | Reduction and protonation of the secondary quinone acceptor of Rhodobacter sphaeroides photosynthetic reaction center: kinetic model based on a comparison of wild-type chromatophores with mutants carrying Arg→Ile substitution at sites 207 and 217 i |
| Q43768969 | Revealing the involvement of extended hydrogen bond networks in the cooperative function between distant sites in bacterial reaction centers |
| Q34996640 | Stigmatellin probes the electrostatic potential in the QB site of the photosynthetic reaction center |
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