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- W835642669 abstract "The reduction.of photo-oxidized reaction center from RhQdos.prilli.um rubrum by c-type cytochromes obtained from horse heart, R. rubrum, and R. capsulata has been investigated. These studies were designed to obtain in formation on a physiological mechanism of electron trans port for O’-type cytochromes and compare these results with available studies with non-physiological reactants. The reaction between c-type cytochromes and re action centers was found to be ionic strength and pH dependent, with electron transfer preceded by complex formation between the reactants« From Debye-Huckel analysis the charge on the reaction center was found to be -4.6 to -4.9 at the site of electron transfer. First-order rate constants, i.e., complex disassociation and electron transfer, were found to be pH and ionic strength independent for R. rubrum cytochrome Cg and horse heart cytochrome c but not R. capsulata .cytochrome £ 2 ° It is concluded that electron transfer takes place at the exposed heme edge. The available data suggests that amino acid side chains distant from the site of electron transfer might be involved in binding the reactants." @default.
- W835642669 created "2016-06-24" @default.
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- W835642669 date "1977-01-01" @default.
- W835642669 modified "2023-09-26" @default.
- W835642669 title "The interaction of c-type cytochromes with Rhodospirillum rubrum reaction centers" @default.
- W835642669 hasPublicationYear "1977" @default.
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