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- W2080443404 abstract "In the transition from the aerobic controlled state to anaerobiosis in rat liver mitochondria with succinate as substrate, cytochrome a3 is reduced prior to cytochrome a, the two components being well separated both in time and in spectral properties. Addition of ATP to anaerobic rat liver mitochondria supplemented with succinate results in 70–80% oxidation of cytochrome a and 10–15% oxidation of cytochrome c+c1 without any measurable change in cytochrome a3. ATP also causes a red shift of 1–1.5 nm in the absorption spectrum of ferrocytochrome a. The shift, which is abolished by uncoupling agents and by oligomycin but is unaffected by cyanide and dithionite, may reflect a molecular event in the energy-conserving mechanism of the terminal “coupling site”." @default.
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- W2080443404 date "1972-11-01" @default.
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- W2080443404 title "Energy-linked change in the redox state and absorption spectrum of cytochrome ain situ" @default.
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- W2080443404 doi "https://doi.org/10.1016/0005-2728(72)90255-1" @default.
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