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- W2054859739 abstract "Molecular O2 and H2O2 acting upon ferrous cytochrome c oxidase (EC 1.9.3.1) appear to form the same compound. Under conditions of complete formation by O2 or by H2O2, the Soret band lies at 427–428 mμ and is of about equal height to the Soret band of the ferric oxidase at 418 mμ. This makes the interpretation of its absorption curve as one of a mixture of ferrous and ferric oxidase untenable. While formation of the 428-mμ compound is complete when 3 moles of H2O2 are added to 1 haem a equivalent of oxidase reduced by 4 moles of dithionite a greater excess of molecular O2 (8–20 moles per mole of haem a) must be added to the gas phase. The 428-mμ compound can, however, be formed under conditions under which no H2O2 is formed by the autoxidation of the reductant, e.g. formamidinosulphinic acid or 1 mole of ferrocytochrome c. The effects of various conditions (standing in air and after evacuation) and reagents (CO, ferricyanide and catalase) are studied. They show that the compound cannot be a reversibly oxygenated compound such as oxyhaemoglobin." @default.
- W2054859739 created "2016-06-24" @default.
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- W2054859739 date "1967-07-01" @default.
- W2054859739 modified "2023-09-27" @default.
- W2054859739 title "Cytochrome oxidase and its derivatives. VII. Further observations on the compound formed by the reaction of ferrous cytochrome c oxidase with oxygen and hydrogen peroxide and on its reactions" @default.
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- W2054859739 doi "https://doi.org/10.1016/0005-2728(67)90107-7" @default.
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