Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli
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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 siteMass spectrometric analysis of the ubiquinol-binding site in cytochrome bd from Escherichia coli.Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode.Oxygenated complex of cytochrome bd from Escherichia coli: stability and photolability.Microsecond time-resolved absorption spectroscopy used to study CO compounds of cytochrome bd from Escherichia coli.The cytochrome bd respiratory oxygen reductasesA Designed Metalloenzyme Achieving the Catalytic Rate of a Native Enzyme.Biogenesis of respiratory cytochromes in bacteria.Cytochrome bd Displays Significant Quinol Peroxidase Activity.Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: A di-heme active site?Direct EPR observation of a tyrosyl radical in a functional oxidase model in myoglobin during both H2O2 and O2 reactions.Cytochrome bd oxidase and nitric oxide: from reaction mechanisms to bacterial physiology.Heme-heme and heme-ligand interactions in the di-heme oxygen-reducing site of cytochrome bd from Escherichia coli revealed by nanosecond absorption spectroscopy.Enterococcus faecalis V583 contains a cytochrome bd-type respiratory oxidase.Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12.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.Oxoferryl-porphyrin radical catalytic intermediate in cytochrome bd oxidases protects cells from formation of reactive oxygen species.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.Arginine 391 in subunit I of the cytochrome bd quinol oxidase from Escherichia coli stabilizes the reduced form of the hemes and is essential for quinol oxidase activity.Further comparison of ubiquinol and cytochrome c terminal oxidases.Cytochrome bd oxidase from Escherichia coli displays high catalase activity: an additional defense against oxidative stress.Nitric oxide reacts with the ferryl-oxo catalytic intermediate of the CuB-lacking cytochrome bd terminal oxidase.Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide.Cytochrome bd oxidase from Azotobacter vinelandii. Purification and quantitation of ligand binding to the oxygen reduction site.Discovery of the true peroxy intermediate in the catalytic cycle of terminal oxidases by real-time measurement
P2860
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P2860
Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli
description
1993 nî lūn-bûn
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1993年の論文
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1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
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1993年学术文章
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1993年学术文章
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1993年學術文章
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1993年學術文章
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1993年學術文章
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name
Spectroscopic evidence for a h ...... oxidase from Escherichia coli
@ast
Spectroscopic evidence for a h ...... oxidase from Escherichia coli
@en
type
label
Spectroscopic evidence for a h ...... oxidase from Escherichia coli
@ast
Spectroscopic evidence for a h ...... oxidase from Escherichia coli
@en
prefLabel
Spectroscopic evidence for a h ...... oxidase from Escherichia coli
@ast
Spectroscopic evidence for a h ...... oxidase from Escherichia coli
@en
P2093
P2860
P356
P1476
Spectroscopic evidence for a h ...... oxidase from Escherichia coli
@en
P2093
P2860
P304
P356
10.1073/PNAS.90.12.5863
P407
P577
1993-06-01T00:00:00Z