C-terminal truncation and histidine-tagging of cytochrome c oxidase subunit II reveals the native processing site, shows involvement of the C-terminus in cytochrome c binding, and improves the assay for proton pumping.
about
Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidaseMass spectrometric detection of protein, lipid and heme components of cytochrome c oxidase from R. sphaeroides and the stabilization of non-covalent complexes from the enzyme.Combined genetic and metabolic manipulation of lipids in Rhodobacter sphaeroides reveals non-phospholipid substitutions in fully active cytochrome c oxidaseRedox-coupled proton translocation in biological systems: proton shuttling in cytochrome c oxidase.Product-controlled steady-state kinetics between cytochrome aa(3) from Rhodobacter sphaeroides and equine ferrocytochrome c analyzed by a novel spectrophotometric approachSpectral identification of intermediates generated during the reaction of dioxygen with the wild-type and EQ(I-286) mutant of Rhodobacter sphaeroides cytochrome c oxidaseCrystallographic location and mutational analysis of Zn and Cd inhibitory sites and role of lipidic carboxylates in rescuing proton path mutants in cytochrome c oxidase.Replacing Asn207 by aspartate at the neck of the D channel in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides results in decoupling the proton pump.Proton-dependent electron transfer from CuA to heme a and altered EPR spectra in mutants close to heme a of cytochrome oxidase.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.Computational prediction and in vitro analysis of potential physiological ligands of the bile acid binding site in cytochrome c oxidaseA conserved amphipathic ligand binding region influences k-path-dependent activity of cytochrome C oxidase.Time-resolved surface-enhanced IR-absorption spectroscopy of direct electron transfer to cytochrome c oxidase from R. sphaeroides.2D-SEIRA spectroscopy to highlight conformational changes of the cytochrome c oxidase induced by direct electron transferPurification of glutamate dehydrogenase from liver and brain.An arginine to lysine mutation in the vicinity of the heme propionates affects the redox potentials of the hemes and associated electron and proton transfer in cytochrome c oxidase.Membrane potential-controlled inhibition of cytochrome c oxidase by zinc.Long distance electron transfer in cytochrome c oxidase immobilised on electrodes. A surface enhanced resonance Raman spectroscopic study.The K-path entrance in cytochrome c oxidase is defined by mutation of E101 and controlled by an adjacent ligand binding domain.
P2860
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P2860
C-terminal truncation and histidine-tagging of cytochrome c oxidase subunit II reveals the native processing site, shows involvement of the C-terminus in cytochrome c binding, and improves the assay for proton pumping.
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
C-terminal truncation and hist ...... the assay for proton pumping.
@ast
C-terminal truncation and hist ...... the assay for proton pumping.
@en
type
label
C-terminal truncation and hist ...... the assay for proton pumping.
@ast
C-terminal truncation and hist ...... the assay for proton pumping.
@en
prefLabel
C-terminal truncation and hist ...... the assay for proton pumping.
@ast
C-terminal truncation and hist ...... the assay for proton pumping.
@en
P2093
P356
P1433
P1476
C-terminal truncation and hist ...... the assay for proton pumping.
@en
P2093
Ferguson-Miller S
P304
P356
10.1021/BI0018988
P407
P577
2001-02-01T00:00:00Z