scholarly article | Q13442814 |
P50 | author | Hiroshi Ishikita | Q37375479 |
Ernst-Walter Knapp | Q47008751 | ||
P2860 | cites work | Electrostatic models for computing protonation and redox equilibria in proteins. | Q52975432 |
Energetics of electron-transfer and protonation reactions of the quinones in the photosynthetic reaction center of Rhodopseudomonas viridis. | Q52996255 | ||
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Tuning electron transfer by ester-group of chlorophylls in bacterial photosynthetic reaction center | Q58199105 | ||
Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers | Q27621441 | ||
Architecture of the photosynthetic oxygen-evolving center | Q27643091 | ||
Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer | Q27736266 | ||
Calculations of electrostatic interactions in biological systems and in solutions | Q29031095 | ||
pKa's of ionizable groups in proteins: atomic detail from a continuum electrostatic model | Q29302657 | ||
Classical electrostatics in biology and chemistry | Q29615082 | ||
Proton uptake by carboxylic acid groups upon photoreduction of the secondary quinone (QB) in bacterial reaction centers from Rhodobacter sphaeroides: FTIR studies on the effects of replacing Glu H173. | Q30431660 | ||
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 pathways and mechanism in bacterial reaction centers | Q35589966 | ||
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 | Q36101981 | ||
Site-specific and compensatory mutations imply unexpected pathways for proton delivery to the QB binding site of the photosynthetic reaction center | Q36562326 | ||
Electrostatic Energy and Macromolecular Function | Q36672066 | ||
Protonation of Glu L212 following QB- formation in the photosynthetic reaction center of Rhodobacter sphaeroides: evidence from time-resolved infrared spectroscopy | Q36720125 | ||
Identification of the proton pathway in bacterial reaction centers: inhibition of proton transfer by binding of Zn2+ or Cd2+. | Q37200776 | ||
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 | ||
The primary acceptor of bacterial photosynthesis: its operating midpoint potential? | Q39085897 | ||
Identification of the proton pathway in bacterial reaction centers: cooperation between Asp-M17 and Asp-L210 facilitates proton transfer to the secondary quinone (QB). | Q43573130 | ||
Retardation of proton transfer caused by binding of the transition metal ion to the bacterial reaction center is due to pKa shifts of key protonatable residues | Q43591642 | ||
Kinetics of electron transfer from Q(a) to Q(b) in photosystem II. | Q43746802 | ||
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 | Q43797215 | ||
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 | Q43809954 | ||
Effect of binding of Cd2+ on bacterial reaction center mutants: proton-transfer uses interdependent pathways | Q44064738 | ||
Redox potential of quinones in photosynthetic reaction centers from Rhodobacter sphaeroides: dependence on protonation of Glu-L212 and Asp-L213. | Q44384214 | ||
Mechanism of proton transfer inhibition by Cd(2+) binding to bacterial reaction centers: determination of the pK(A) of functionally important histidine residues | Q44544841 | ||
Redox potential of quinones in both electron transfer branches of photosystem I. | Q44583881 | ||
X-Ray structure determination of three mutants of the bacterial photosynthetic reaction centers from Rb. sphaeroides; altered proton transfer pathways | Q44828373 | ||
Variation of Ser-L223 hydrogen bonding with the QB redox state in reaction centers from Rhodobacter sphaeroides | Q44948314 | ||
Redox potentials of chlorophylls and beta-carotene in the antenna complexes of photosystem II. | Q45257649 | ||
Protons forge new paths. | Q47828297 | ||
A new metal-binding site in photosynthetic bacterial reaction centers that modulates QA to QB electron transfer | Q47986471 | ||
Electron transfer between the quinones in the photosynthetic reaction center and its coupling to conformational changes. | Q51644690 | ||
Tuning heme redox potentials in the cytochrome C subunit of photosynthetic reaction centers. | Q52009231 | ||
Calculated protein and proton motions coupled to electron transfer: electron transfer from QA- to QB in bacterial photosynthetic reaction centers. | Q52210542 | ||
P433 | issue | 13 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Rhodobacter sphaeroides | Q4186823 |
P1104 | number of pages | 5 | |
P304 | page(s) | 12446-12450 | |
P577 | publication date | 2005-01-06 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Energetics of proton transfer pathways in reaction centers from Rhodobacter sphaeroides. The Glu-H173 activated mutants | |
P478 | volume | 280 |
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