| scholarly article | Q13442814 |
| P819 | ADS bibcode | 1989PNAS...86.6602P |
| P356 | DOI | 10.1073/PNAS.86.17.6602 |
| P932 | PMC publication ID | 297892 |
| P698 | PubMed publication ID | 2570421 |
| P5875 | ResearchGate publication ID | 20586591 |
| P50 | author | George Feher | Q1507337 |
| P2093 | author name string | M Y Okamura | |
| M L Paddock | |||
| S H Rongey | |||
| P2860 | cites work | Cleavage by the restriction endonuclease Asp718, an isoschizomer of KpnI, is sensitive to Escherichia coli Dcm methylation | Q24632142 |
| The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers | Q28131744 | ||
| Production of single-stranded plasmid DNA | Q29547328 | ||
| Aspartic acid substitutions affect proton translocation by bacteriorhodopsin | Q33580073 | ||
| Structure of the reaction center from Rhodobacter sphaeroides R-26: protein-cofactor (quinones and Fe2+) interactions | Q33670297 | ||
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| Electron acceptors of bacterial photosynthetic reaction centers II. H+ binding coupled to secondary electron transfer in the quinone acceptor complex | Q39286158 | ||
| Transfer of chromosomal genes mediated by plasmid r68.45 in Rhodopseudomonas sphaeroides | Q40034642 | ||
| Hydrogen bonded chain mechanisms for proton conduction and proton pumping | Q40135648 | ||
| A Rhodobacter sphaeroides puf L, M and X deletion mutant and its complementation in trans with a 5.3 kb puf operon shuttle fragment. | Q40816873 | ||
| Interaction between Glu-219 and His-245 within the a subunit of F1F0-ATPase in Escherichia coli | Q46408763 | ||
| Proton conduction through proteins: an overview of theoretical principles and applications. | Q52655029 | ||
| 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 | ||
| Chromosomal deletion and plasmid complementation of the photosynthetic reaction center and light-harvesting genes from Rhodopseudomonas capsulata | Q69848658 | ||
| lac permease of Escherichia coli: histidine-322 and glutamic acid-325 may be components of a charge-relay system | Q69888321 | ||
| Plasmids related to the broad host range vector, pRK290, useful for gene cloning and for monitoring gene expression | Q70087619 | ||
| P433 | issue | 17 | |
| P407 | language of work or name | English | Q1860 |
| P1104 | number of pages | 5 | |
| P304 | page(s) | 6602-6606 | |
| P577 | publication date | 1989-09-01 | |
| P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
| P1476 | title | Pathway of proton transfer in bacterial reaction centers: replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover | |
| P478 | volume | 86 |
| Q73374261 | A native electrostatic environment near Q(B) is not sufficient to ensure rapid proton delivery in photosynthetic reaction centers |
| Q30326804 | A pragmatic approach to structure based calculation of coupled proton and electron transfer in proteins. |
| Q41517483 | A system for site-specific mutagenesis of the photosynthetic reaction center in Rhodopseudomonas viridis |
| Q78207975 | An Escherichia coli mutant quinol:fumarate reductase contains an EPR-detectable semiquinone stabilized at the proximal quinone-binding site |
| Q43069600 | Analysis of the electrochemistry of hemes with E(m)s spanning 800 mV. |
| Q59033053 | Atavistic reaction centre |
| Q33225243 | B-branch electron transfer in reaction centers of Rhodobacter sphaeroides assessed with site-directed mutagenesis |
| Q81358369 | Characterization of a symmetrized mutant RC with 42 residues from the QA site replacing residues in the Q(B) site |
| Q95297494 | Characterization of the photoreduction of the secondary quinone QB in the photosynthetic reaction center from rhodobacter capsulatus with FTIR spectroscopy |
| Q86892592 | Comparative study of reaction centers from purple photosynthetic bacteria: Isolation and optical spectroscopy |
| Q33801133 | Conformationally controlled pK-switching in membrane proteins: one more mechanism specific to the enzyme catalysis? |
| Q33855885 | Cooperative effect of two surface amino acid mutations (Q252L and E170K) in glucose dehydrogenase from Bacillus megaterium IWG3 on stabilization of its oligomeric state |
| Q27621441 | Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers |
| Q30052790 | Electrostatic calculations of amino acid titration and electron transfer, Q-AQB-->QAQ-B, in the reaction center |
| Q37607518 | Electrostatic control of midpoint potentials in the cytochrome subunit of the Rhodopseudomonas viridis reaction center |
| Q45214716 | Energetics of proton transfer pathways in reaction centers from Rhodobacter sphaeroides. The Glu-H173 activated mutants |
| Q47713248 | Energy trapping and detrapping by wild type and mutant reaction centers of purple non-sulfur bacteria |
| Q54245085 | Evidence that serine L223 is involved in the proton transfer pathway to QB in the photosynthetic reaction center of Rhodopseudomonas viridis. |
| Q77360111 | Flash-induced changes in buffering capacity of reaction centers from photosynthetic bacteria reveal complex interaction between quinone pockets |
| Q72315431 | Flash-induced electrogenic reactions in the SA(L223) reaction center mutant in Rhodobacter sphaeroides chromatophores |
| Q86911961 | Flash-induced proton transfer in photosynthetic bacteria |
| Q44387204 | George Feher: a pioneer in reaction center research |
| Q42173725 | Identification of FTIR bands due to internal water molecules around the quinone binding sites in the reaction center from Rhodobacter sphaeroides |
| Q37282071 | Identification of the proton pathway in bacterial reaction centers: both protons associated with reduction of QB to QBH2 share a common entry point |
| Q37200776 | Identification of the proton pathway in bacterial reaction centers: inhibition of proton transfer by binding of Zn2+ or Cd2+. |
| Q31514386 | 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+. |
| Q34132176 | Induced conformational changes upon Cd2+ binding at photosynthetic reaction centers |
| Q87091322 | Inhibition and labelling of isolated reaction centers from Rhodobacter sphaeroides by dicyclohexylcarbodiimide |
| Q29542853 | Investigating the mechanisms of photosynthetic proteins using continuum electrostatics |
| Q81773006 | Investigation of ubiquinol formation in isolated photosynthetic reaction centers by rapid-scan Fourier transform IR spectroscopy |
| Q33907060 | Kinetics of H+ ion binding by the P+QA-state of bacterial photosynthetic reaction centers: rate limitation within the protein |
| Q73793536 | Light-induced electrogenic events associated with proton uptake upon forming QB- in bacterial wild-type and mutant reaction centers |
| Q71625897 | Long-range electrostatic interaction in the bacterial photosynthetic reaction centre |
| Q36145875 | Membrane topography of ColE1 gene products: the hydrophobic anchor of the colicin E1 channel is a helical hairpin |
| Q39503006 | Mobile cytochrome c2 and membrane-anchored cytochrome cy are both efficient electron donors to the cbb3- and aa3-type cytochrome c oxidases during respiratory growth of Rhodobacter sphaeroides. |
| Q28287439 | Molecular mechanisms for generating transmembrane proton gradients |
| Q33773605 | 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 |
| Q36101981 | 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 |
| Q38078298 | Photosynthetic reaction center-functionalized electrodes for photo-bioelectrochemical cells |
| Q37669865 | 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 |
| Q33919268 | Proton and electron transfer in bacterial reaction centers |
| Q35505196 | Proton conduction within the reaction centers of Rhodobacter capsulatus: the electrostatic role of the protein |
| Q44476887 | Proton release upon oxidation of tyrosine in reaction centers from Rhodobacter sphaeroides |
| Q47366693 | Proton transfer from H₂O to p-substituted anilide anion: can the size of water cluster influence the N⁻···H-OH→N-H···OH⁻ switching |
| Q35589966 | Proton transfer pathways and mechanism in bacterial reaction centers |
| Q36744804 | Proton uptake by bacterial reaction centers: the protein complex responds in a similar manner to the reduction of either quinone acceptor |
| Q43984323 | Rapid-scan Fourier transform infrared spectroscopy shows coupling of GLu-L212 protonation and electron transfer to Q(B) in Rhodobacter sphaeroides reaction centers |
| Q45189152 | Reaction centers from three herbicide resistant mutants of Rhodobacter sphaeroides 2.4.1: Kinetics of electron transfer reactions |
| 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 |
| Q33712714 | Relationship between the oxidation potential and electron spin density of the primary electron donor in reaction centers from Rhodobacter sphaeroides |
| Q33193296 | Residual Water Modulates QA−-to-QB Electron Transfer in Bacterial Reaction Centers Embedded in Trehalose Amorphous Matrices |
| Q87065956 | Second-site mutation at M43 (Asn→Asp) compensates for the loss of two acidic residues in the QB site of the reaction center |
| Q33836882 | Simple redox-linked proton-transfer design: new insights from structures of quinol-fumarate reductase |
| Q36562326 | Site-specific and compensatory mutations imply unexpected pathways for proton delivery to the QB binding site of the photosynthetic reaction center |
| Q68237527 | Small weak acids stimulate proton transfer events in site-directed mutants of the two ionizable residues, GluL212 and AspL213, in the QB-binding site of Rhodobacter sphaeroides reaction center |
| Q35845034 | Specific alteration of the oxidation potential of the electron donor in reaction centers from Rhodobacter sphaeroides |
| Q86901105 | Spectroscopic characterization of reaction centers of the (M)Y210W mutant of the photosynthetic bacterium Rhodobacter sphaeroides |
| Q34329955 | Structure and function of the photosynthetic reaction center from Rhodobacter sphaeroides |
| Q34019516 | Study of wild type and genetically modified reaction centers from Rhodobacter capsulatus: structural comparison with Rhodopseudomonas viridis and Rhodobacter sphaeroides |
| Q43801649 | Substitution of valine-157 residue by tyrosine in the L-subunit of the Rhodobacter sphaeroides reaction center |
| Q33956966 | Succinate dehydrogenase and fumarate reductase from Escherichia coli |
| Q58047838 | Temperature dependence of the electrogenic reaction in the QB site of the Rhodobacter sphaeroides photosynthetic reaction center: the QA − QB →QA QB − transition |
| Q47708947 | The Ile(L229) → Met mutation impairs the quinone binding to the QB-pocket in reaction centers of Rhodobacter sphaeroides |
| Q43560191 | The Quinone-binding sites of the Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase |
| Q24674125 | The heme redox center of chloroplast cytochrome f is linked to a buried five-water chain |
| Q35125024 | The membrane-attached electron carrier cytochrome cy from Rhodobacter sphaeroides is functional in respiratory but not in photosynthetic electron transfer |
| Q38098080 | The three-dimensional structures of bacterial reaction centers |
| Q81575815 | Time line of discoveries: anoxygenic bacterial photosynthesis |
| Q50909081 | Use of new strains of Rhodobacter sphaeroides and a modified simple culture medium to increase yield and facilitate purification of the reaction centre. |
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