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• W2166407223 endingPage "1344" @default.
• W2166407223 startingPage "1335" @default.
• W2166407223 abstract "The form of cytochrome d in Escherichia coli and Azotobacter vinelandii that shows an absorption maximum at 648 to 652 nm (cytochrome d 650) is generally regarded as the oxidized form of this terminal oxidase. Membranes from E. coli grown under oxygen-limited conditions, when treated with ferricyanide, do not reveal cytochrome d 650, whereas a sharp symmetrical band at 652 nm results from the reaction of the reduced enzyme with O2 at either room temperature or after flash photolysis of the CO-liganded form at 130 C. Electron paramagnetic resonance spectroscopy of cytochrome d 650 trapped at 130 C shows that its spectrum is indistinguishable from the CO-liganded form and does not reveal resonances of high spin ferric haem previously attributed to cytochrome d. An hypothesis is proposed in which cytochrome d 650 is an early intermediate in the reaction of reduced cytochrome d with oxygen and is not the fully-oxidized (ferric) species. An analogy between cytochrome d 650 and oxyhaemoglobin is presented and the hypothesis discussed in relation to earlier work, in which the indirect interconversions of reduced cytochrome d and d 650 have been explained by proposing the existence of an invisible form. It is suggested that this form could be the oxidized enzyme." @default.
• W2166407223 created "2016-06-24" @default.
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• W2166407223 date "1983-05-01" @default.
• W2166407223 modified "2023-09-26" @default.
• W2166407223 title "The 650 nm Chromophore in Escherichia coli is an 'Oxy-' or Oxygenated Compound, Not the Oxidized Form of Cytochrome Oxidase d: An Hypothesis" @default.
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• W2166407223 doi "https://doi.org/10.1099/00221287-129-5-1335" @default.
• W2166407223 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6311941" @default.
• W2166407223 hasPublicationYear "1983" @default.
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