Coulometric and spectroscopic analysis of the purified cytochrome d complex of Escherichia coli: evidence for the identification of "cytochrome a1" as cytochrome b595.
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Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active siteCharacterization of the cydAB-encoded cytochrome bd oxidase from Mycobacterium smegmatis.Characterization of the type 2 NADH:menaquinone oxidoreductases from Staphylococcus aureus and the bactericidal action of phenothiazinesCytochrome a1 of acetobacter aceti is a cytochrome ba functioning as ubiquinol oxidaseCloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: mutants deficient in the cytochrome d complex are unable to fix nitrogen in airMicrosecond time-resolved absorption spectroscopy used to study CO compounds of cytochrome bd from Escherichia coli.The cytochrome bd respiratory oxygen reductasesIsolation and characterization of a new class of cytochrome d terminal oxidase mutants of Escherichia coliCloning, characterization, and expression in Escherichia coli of the genes encoding the cytochrome d oxidase complex from Azotobacter vinelandii.Identification of the cydC locus required for expression of the functional form of the cytochrome d terminal oxidase complex in Escherichia coli.Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coliNMR and EPR studies of chloroiron(III) tetraphenyl-chlorin and its complexes with imidazoles and pyridines of widely differing basicities.The fully oxidized form of the cytochrome bd quinol oxidase from E. coli does not participate in the catalytic cycle: direct evidence from rapid kinetics studies.Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: A di-heme active site?Heme-heme and heme-ligand interactions in the di-heme oxygen-reducing site of cytochrome bd from Escherichia coli revealed by nanosecond absorption spectroscopy.Purification and characterization of the cytochrome bd complex from Azotobacter vinelandii: comparison to the complex from Escherichia coli.Evidence for Fast Electron Transfer between the High-Spin Haems in Cytochrome bd-I from Escherichia coli.Proposal that the function of the membrane-bound cytochrome a1-like haemoprotein (cytochrome b-595) in Escherichia coli is a direct electron donation to cytochrome d.The cytochromes of anaerobically grown Escherichia coli. An electron-paramagnetic-resonance study of the cytochrome bd complex in situ.The haem b558 component of the cytochrome bd quinol oxidase complex from Escherichia coli has histidine-methionine axial ligation.The orientation of the three haems of the 'in situ' ubiquinol oxidase, cytochrome bd, of Escherichia coli.Gene fusions with beta-lactamase show that subunit I of the cytochrome bd quinol oxidase from E. coli has nine transmembrane helices with the O2 reactive site near the periplasmic surface.Intracellular expression of Vitreoscilla hemoglobin modifies microaerobic Escherichia coli metabolism through elevated concentration and specific activity of cytochrome o.Intracellular expression of Vitreoscilla hemoglobin modifies microaerobic Escherichia coli metabolism through elevated concentration and specific activity of cytochrome o.Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide.The highly conserved methionine of subunit I of the heme-copper oxidases is not at the heme-copper dinuclear center: mutagenesis of M110 in subunit I of cytochrome bo3-type ubiquinol oxidase from Escherichia coli.Cytochrome bd oxidase from Azotobacter vinelandii. Purification and quantitation of ligand binding to the oxygen reduction site.Antimycin inhibition of the cytochrome bd complex from Azotobacter vinelandii indicates the presence of a branched electron transfer pathway for the oxidation of ubiquinol.Discovery of the true peroxy intermediate in the catalytic cycle of terminal oxidases by real-time measurement
P2860
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P2860
Coulometric and spectroscopic analysis of the purified cytochrome d complex of Escherichia coli: evidence for the identification of "cytochrome a1" as cytochrome b595.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年学术文章
@wuu
1986年学术文章
@zh-cn
1986年学术文章
@zh-hans
1986年学术文章
@zh-my
1986年学术文章
@zh-sg
1986年學術文章
@yue
1986年學術文章
@zh
1986年學術文章
@zh-hant
name
Coulometric and spectroscopic ...... chrome a1" as cytochrome b595.
@en
Coulometric and spectroscopic ...... chrome a1" as cytochrome b595.
@nl
type
label
Coulometric and spectroscopic ...... chrome a1" as cytochrome b595.
@en
Coulometric and spectroscopic ...... chrome a1" as cytochrome b595.
@nl
prefLabel
Coulometric and spectroscopic ...... chrome a1" as cytochrome b595.
@en
Coulometric and spectroscopic ...... chrome a1" as cytochrome b595.
@nl
P356
P1433
P1476
Coulometric and spectroscopic ...... ochrome a1" as cytochrome b595
@en
P2093
R B Gennis
R M Lorence
P304
P356
10.1021/BI00357A003
P407
P577
1986-05-01T00:00:00Z