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• W85873273 abstract "SUMMARY The function of cytochrome c in the electron-transport chain is validated by the observations of its oxidation in a time of 8 msec in the uncoupled state, and a value of over 25 msec in the coupled state. Cytochrome c is apparently a part of a redox-buffered pool which needs the specificity requirements of both cytochrome c1 and a and operates between energy coupling site III (a3)(17) and II (T if indeed it operates as a pool, some increase or decrease would not alter the function of the membrane. The location of cytochrome c on the outside surface of the inner membrane, together with cytochrome c peroxidase in yeast mitochondria and accessible to this oxidant in intact mitochondria if the outer membrane is removed, affords a peripheral location which allows assembly of cytochromes in the membrane following membrane biosynthesis. Furthermore, the multiplicity of binding sites permits the acquisition of variable amounts of cytochrome c depending upon the amount synthesized. Thus it is apparent that the electron-donating site of cytochrome c is not buried in the membrane, but rather accessible to the membrane-bound oxidase, and, in yeast mitochondria, to the membrane-bound peroxidase as well. In this location, cytochrome c has a reasonable translational and rotational mobility, so that its active region may be alternatively accessible to both oxidases. The failure of cytochrome c to exhibit redox equilibration at rates equal to those observed in the membrane suggests that there is a catalyst for the equilibration in the membrane reaction." @default.
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• W85873273 date "1972-01-01" @default.
• W85873273 modified "2023-10-17" @default.
• W85873273 title "THE FUNCTION OF CYTOCHROME c IN MITOCHONDRIAL MEMBRANES" @default.
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• W85873273 doi "https://doi.org/10.1016/b978-0-08-016874-6.50036-9" @default.
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