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.
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Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centersMolecular mechanisms for generating transmembrane proton gradientsElectrostatic calculations of amino acid titration and electron transfer, Q-AQB-->QAQ-B, in the reaction centerIdentification 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+.Residual water modulates QA- -to-QB electron transfer in bacterial reaction centers embedded in trehalose amorphous matrices.Conformationally controlled pK-switching in membrane proteins: one more mechanism specific to the enzyme catalysis?Kinetics of H+ ion binding by the P+QA-state of bacterial photosynthetic reaction centers: rate limitation within the proteinPhotoelectrochemical complexes for solar energy conversion that chemically and autonomously regenerate.Study of wild type and genetically modified reaction centers from Rhodobacter capsulatus: structural comparison with Rhodopseudomonas viridis and Rhodobacter sphaeroides.Key role of proline L209 in connecting the distant quinone pockets in the reaction center of Rhodobacter sphaeroides.Induced conformational changes upon Cd2+ binding at photosynthetic reaction centersStigmatellin probes the electrostatic potential in the QB site of the photosynthetic reaction center.Proton conduction within the reaction centers of Rhodobacter capsulatus: the electrostatic role of the proteinProton transfer pathways and mechanism in bacterial reaction centers.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.Site-specific and compensatory mutations imply unexpected pathways for proton delivery to the QB binding site of the photosynthetic reaction center.Proton uptake by bacterial reaction centers: the protein complex responds in a similar manner to the reduction of either quinone acceptorCoupling of cytochrome and quinone turnovers in the photocycle of reaction centers from the photosynthetic bacterium Rhodobacter sphaeroides.Identification of the proton pathway in bacterial reaction centers: inhibition of proton transfer by binding of Zn2+ or Cd2+.Identification of the proton pathway in bacterial reaction centers: both protons associated with reduction of QB to QBH2 share a common entry pointPotentiation of proton transfer function by electrostatic interactions in photosynthetic reaction centers from Rhodobacter sphaeroides: First results from site-directed mutation of the H subunit.Functions of the hydrophilic channels in protonmotive cytochrome c oxidase.The two last overviews by Colin Allen Wraight (1945-2014) on energy conversion in photosynthetic bacteria.Photosynthetic electron transfer controlled by protein relaxation: analysis by Langevin stochastic approach.Multiple scattering x-ray absorption studies of Zn2+ binding sites in bacterial photosynthetic reaction centers.Electronic pathway in reaction centers from Rhodobacter sphaeroides and Chloroflexus aurantiacus.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.Identification of FTIR bands due to internal water molecules around the quinone binding sites in the reaction center from Rhodobacter sphaeroides.DCCD inhibits the reactions of the iron-sulfur protein in Rhodobacter sphaeroides chromatophores.The DMPC lipid phase transition influences differently the first and the second electron transfer reactions in bacterial reaction centers.Characteristics and reactivity of ruthenium-oxo complexes.The respiratory substrate rhodoquinol induces Q-cycle bypass reactions in the yeast cytochrome bc(1) complex: mechanistic and physiological implications.Colin A. Wraight, 1945-2014.Temperature dependence of the electrogenic reaction in the QB site of the Rhodobacter sphaeroides photosynthetic reaction center: the QA − QB →QA QB − transition
P2860
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P2860
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.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh-hant
name
Proton and electron transfer i ...... pL213, in the QB binding site.
@en
Proton and electron transfer i ...... pL213, in the QB binding site.
@nl
type
label
Proton and electron transfer i ...... pL213, in the QB binding site.
@en
Proton and electron transfer i ...... pL213, in the QB binding site.
@nl
prefLabel
Proton and electron transfer i ...... pL213, in the QB binding site.
@en
Proton and electron transfer i ...... pL213, in the QB binding site.
@nl
P356
P1433
P1476
Proton and electron transfer i ...... pL213, in the QB binding site.
@en
P2093
Takahashi E
Wraight CA
P304
P356
10.1021/BI00118A031
P407
P577
1992-01-01T00:00:00Z