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The cytochrome bd respiratory oxygen reductases.
Cytochrome bd is a respiratory quinol: O₂ oxidoreductase found in many prokaryotes, including a number of pathogens. The main bioenergetic function of the enzyme is the production of a proton motiveExpand
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Cytochrome bd oxidase and bacterial tolerance to oxidative and nitrosative stress.
Cytochrome bd is a prokaryotic respiratory quinol:O2 oxidoreductase, phylogenetically unrelated to the extensively studied heme-copper oxidases (HCOs). The enzyme contributes to energy conservationExpand
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Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode
Escherichia coli is known to couple aerobic respiratory catabolism to ATP synthesis by virtue of the primary generators of the proton motive force—NADH dehydrogenase I, cytochrome bo3, and cytochromeExpand
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Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide
Cytochrome bd is a prokaryotic terminal oxidase catalyzing O2 reduction to H2O. The oxygen‐reducing site has been proposed to contain two hemes, d and b 595, the latter presumably replacingExpand
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Strong excitonic interactions in the oxygen-reducing site of bd-type oxidase: the Fe-to-Fe distance between hemes d and b595 is 10 A.
Absorption and circular dichroism (CD) spectra of cytochrome bd from Escherichia coli have been compared for the wild type enzyme and an inactive mutant in which a highly conserved E445 in subunit IExpand
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The Terminal Oxidase Cytochrome bd Promotes Sulfide-resistant Bacterial Respiration and Growth
Hydrogen sulfide (H2S) impairs mitochondrial respiration by potently inhibiting the heme-copper cytochrome c oxidase. Since many prokaryotes, including Escherichia (E.) coli, generate H2S andExpand
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Defects in mitochondrial respiratory complexes III and IV, and human pathologies.
  • V. Borisov
  • Biology, Medicine
  • Molecular aspects of medicine
  • 1 October 2002
Here, relationships between alterations in tissue-specific content, protein structure, activity, and/or assembly of respiratory complexes III and IV induced by mutations in corresponding genes andExpand
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Oxygen as Acceptor.
Like most bacteria, Escherichia coli has a flexible and branched respiratory chain that enables the prokaryote to live under a variety of environmental conditions, from highly aerobic to completelyExpand
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Redox control of fast ligand dissociation from Escherichia coli cytochrome bd.
Bacterial bd-type quinol oxidases, such as cytochrome bd from Escherichia coli, contain three hemes, but no copper. In contrast to heme-copper oxidases and similarly to globins, singleExpand
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Interactions between heme d and heme b595 in quinol oxidase bd from Escherichia coli: a photoselection study using femtosecond spectroscopy.
Femtosecond spectroscopy was performed on CO-liganded (fully reduced and mixed-valence states) and O(2)-liganded quinol oxidase bd from Escherichia coli. Substantial polarization effects,Expand
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