
Journal of Physical Chemistry p. 8023 - 8027 (1992)
Update date:2022-08-10
Topics:
Larsen, Randy W.
Winkler, Jay R.
Chan, Sunney I.
We have employed a novel photoreduction system to investigate the electron-transfer reaction between cytochrome c and cytochrome c oxidase.In this system, the photogenerated uroporphyrin triplet state is quenched through electron transfer to ferricytochrome c.The corresponding uroporphyrin ?-cation radical is rapidly reduced by nicotonamid adenine dinucleotide (NADH) resulting in the in situ generation of ferrocytochrome c.In the presence of cytochrome c oxidase, cytochrome c is reoxidized biphasically while the corresponding reduction of cytochrome a appears to be monophasic.In addition, the fast-phase rate constants are dependent upon the concentration of cytochrome c oxidase giving a first-order intracomplex electron-transfer rate constant, (ket), of 1829 +/-248 s-1.The ratio of electron transferred from ferrocytochrome c to cytochrome a is 1:1 indicating that cytochrome a is the ultimate acceptor of the electrons.
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