Abstract
Zinc-substituted cytochrome c, Zn cyt c, in which the heme iron atom is substituted by Zn(II), has been used in a number of basic studies of electron-transfer reactions of proteins. In this paper we report detailed studies of the ground-state and excited-state redox behavior of Zn cyt c which provide experimental estimates of key parameters including the oxidation potential (Zn cyt c)/Zn c, E° ≅ 0.8 V, and the (relative) reaction rates of Zn cyt c/Fe cyt c with a common reactant (corrected for reaction ΔG), k11(Zn)/k11(Fe) = 5 ± 1. The implications of these results for electron-transfer studies of proteins are briefly discussed.
Original language | English (Ireland) |
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Pages (from-to) | 7130-7134 |
Number of pages | 5 |
Journal | Journal of Physical Chemistry |
Volume | 93 |
Issue number | 20 |
DOIs | |
Publication status | Published - 1989 |