Properties of Arg481 mutants of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that neither R481 nor the nearby D-propionate of heme a3 is likely to be the proton loading site of the proton pump.
about
Proton-coupled electron transferMultiscale simulations reveal key features of the proton-pumping mechanism in cytochrome c oxidaseMicroscopic basis for kinetic gating in Cytochrome c oxidase: insights from QM/MM analysis.Exploration of the cytochrome c oxidase pathway puzzle and examination of the origin of elusive mutational effects.Blocking the K-pathway still allows rapid one-electron reduction of the binuclear center during the anaerobic reduction of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides.Expanding the view of proton pumping in cytochrome c oxidase through computer simulation.Functional interactions between membrane-bound transporters and membranes.Spectral components of the α-band of cytochrome oxidaseFunctional and structural roles of residues in the third extramembrane segment of adrenal cytochrome b561.Glu-286 rotation and water wire reorientation are unlikely the gating elements for proton pumping in cytochrome C oxidase.Entrance of the proton pathway in cbb3-type heme-copper oxidases.Exploring the proton pump and exit pathway for pumped protons in cytochrome ba3 from Thermus thermophilus.Radical formation in cytochrome c oxidaseCommunication between R481 and Cu(B) in cytochrome bo(3) ubiquinol oxidase from Escherichia coli.Computational prediction and in vitro analysis of potential physiological ligands of the bile acid binding site in cytochrome c oxidaseCoupled electron and proton transfer reactions during the O→E transition in bovine cytochrome c oxidase.Current advances in research of cytochrome c oxidase.Proton-transport mechanisms in cytochrome c oxidase revealed by studies of kinetic isotope effects.
P2860
Q24597113-2C9E5C07-CE99-4614-8603-216671271C17Q28830505-527B77D7-FC27-4AAE-8CF5-70A2A892B73FQ30394639-A13DF731-6A96-4DDA-966E-76E239E58409Q33350451-DE78AE50-7B5E-4E25-8EF0-7C1277E93A73Q33936331-0961449B-EBDF-4757-B7CC-FB553C7E6AC0Q33998203-5AB8C40C-2A09-4DAB-81A3-E9D9CFBCDB06Q34115431-83D3497C-771C-4C0C-8876-D3F70EEFDD93Q34995578-FFE51941-10AB-490F-9AB6-E3909DC0D02BQ34997575-FB0A3771-16DB-4A26-8DCA-9A21BFCC23D8Q35079430-AAE7E8ED-B079-470B-9063-04D4E8243F17Q35470860-E08C1A8F-D625-4EC4-AFA1-A7D4FD7E3675Q35887138-769ACC50-5BE2-4138-BCB6-A6BA6C495B7CQ35966416-999DCE83-6C39-41BC-A6FD-5CF3E324DA52Q36163371-8B4CBF67-30A5-4439-BA76-9AC24F33AB2EQ37384663-EC95871C-DF0A-4DCC-92B2-8E5BAD700685Q37956518-9E9E3A92-AF1E-4AD1-8D64-37965CD3C381Q38133739-365FFB51-4AD1-4A4D-9B1F-2A601CF627D7Q42829146-C29B99F3-33A6-4D9E-86DC-3EFE62B77CE5
P2860
Properties of Arg481 mutants of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that neither R481 nor the nearby D-propionate of heme a3 is likely to be the proton loading site of the proton pump.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on August 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Properties of Arg481 mutants o ...... ading site of the proton pump.
@en
Properties of Arg481 mutants o ...... ading site of the proton pump.
@nl
type
label
Properties of Arg481 mutants o ...... ading site of the proton pump.
@en
Properties of Arg481 mutants o ...... ading site of the proton pump.
@nl
prefLabel
Properties of Arg481 mutants o ...... ading site of the proton pump.
@en
Properties of Arg481 mutants o ...... ading site of the proton pump.
@nl
P2093
P2860
P356
P1433
P1476
Properties of Arg481 mutants o ...... ading site of the proton pump.
@en
P2093
Ahmet Vakkasoglu
Hyun Ju Lee
Linda Ojemyr
Robert B Gennis
P2860
P304
P356
10.1021/BI901015D
P407
P577
2009-08-01T00:00:00Z