Identification of the proton pathway in bacterial reaction centers: inhibition of proton transfer by binding of Zn2+ or Cd2+.
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Energy transduction: proton transfer through the respiratory complexesDetermination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centersA histidine residue acting as a controlling site for dioxygen reduction and proton pumping by cytochrome c oxidaseEffects of Zinc on Particulate Methane Monooxygenase Activity and StructureMolecular mechanisms for generating transmembrane proton gradientsIdentification 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+.Role of the H protein in assembly of the photochemical reaction center and intracytoplasmic membrane in Rhodospirillum rubrum.Induced conformational changes upon Cd2+ binding at photosynthetic reaction centersDiscovery of a reaction intermediate of aliphatic aldoxime dehydratase involving heme as an active center.Proton transfer pathways and mechanism in bacterial reaction centers.X-Ray absorption studies of Zn2+ binding sites in bacterial, avian, and bovine cytochrome bc1 complexes.Identification of the proton pathway in bacterial reaction centers: both protons associated with reduction of QB to QBH2 share a common entry pointMultiple scattering x-ray absorption studies of Zn2+ binding sites in bacterial photosynthetic reaction centers.The cytochrome b Zn binding amino acid residue histidine 291 is essential for ubihydroquinone oxidation at the Qo site of bacterial cytochrome bc1.Zinc ions inhibit oxidation of cytochrome c oxidase by oxygen.Membrane potential-controlled inhibition of cytochrome c oxidase by zinc.Energetics of proton transfer pathways in reaction centers from Rhodobacter sphaeroides. The Glu-H173 activated mutants.Exploring the primary electron acceptor (QA)-site of the bacterial reaction center from Rhodobacter sphaeroides. Binding mode of vitamin K derivatives.Reversible Anion-Driven Switching of an Organic 2D Crystal at a Solid-Liquid Interface.Characterization of mercury(II)-induced inhibition of photochemistry in the reaction center of photosynthetic bacteria.Thermally Induced Intra-Carboxyl Proton Shuttle in a Molecular Rack-and-Pinion Cascade Achieving Macroscopic Crystal Deformation.Antimicrobial efficacy of a silver-zeolite matrix coating on stainless steel.
P2860
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P2860
Identification of the proton pathway in bacterial reaction centers: inhibition of proton transfer by binding of Zn2+ or Cd2+.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 1999
@en
vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Identification of the proton p ...... er by binding of Zn2+ or Cd2+.
@en
Identification of the proton p ...... er by binding of Zn2+ or Cd2+.
@nl
type
label
Identification of the proton p ...... er by binding of Zn2+ or Cd2+.
@en
Identification of the proton p ...... er by binding of Zn2+ or Cd2+.
@nl
prefLabel
Identification of the proton p ...... er by binding of Zn2+ or Cd2+.
@en
Identification of the proton p ...... er by binding of Zn2+ or Cd2+.
@nl
P2093
P2860
P356
P1476
Identification of the proton p ...... er by binding of Zn2+ or Cd2+.
@en
P2093
M L Paddock
M S Graige
M Y Okamura
P2860
P304
P356
10.1073/PNAS.96.11.6183
P407
P577
1999-05-01T00:00:00Z