PMID: 9526032Apr 4, 1998Paper

Ferrocyanide-peroxidase activity of cytochrome c oxidase

Biochimica Et Biophysica Acta
Alexander A KonstantinovS Papa

Abstract

Redox interaction of mitochondrial cytochrome c oxidase (COX) with ferrocyanide/ferricyanide couple is greatly accelerated by polycations, such as poly-l-lysine [Musatov et al. (1991) Biological Membranes 8, 229-234]. This has allowed us to study ferrocyanide oxidation by COX at very high redox potentials of the ferrocyanide/ferricyanide couple either following spectrophotometrically ferricyanide accumulation or measuring proton uptake associated with water formation in the reaction. At low [ferrocyanide]/[ferricyanide] ratios (Eh values around 500 mV) and ambient oxygen concentration, the ferrocyanide-oxidase activity of COX becomes negligibly small as compared to the reaction rate observed with pure ferrocyanide. Oxidation of ferrocyanide under these conditions, is greatly stimulated by H2O2 or ethylhydroperoxide indicating peroxidatic reaction involved. The ferrocyanide-peroxidase activity of COX is strictly polylysine-dependent and is inhibited by heme a3 ligands such as KCN and NaN3. Apparently the reaction involves normal electron pathway, i.e. electron donation through CuA and oxidation via heme a3. The peroxidase reaction shows a pH-dependence similar to that of the cytochrome c oxidase activity of COX. When COX is pree...Continue Reading

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Citations

Nov 21, 2007·Biochemistry. Biokhimii︠a︡·P R Rich, M Iwaki
Nov 21, 2007·Biochemistry. Biokhimii︠a︡·T V Vygodina, A A Konstantinov
Jul 14, 2010·Biochemistry. Biokhimii︠a︡·V B BorisovA A Konstantinov
Aug 30, 2011·Biochimica Et Biophysica Acta·Sergey A Siletsky, Alexander A Konstantinov
Mar 7, 2021·Archives of Biochemistry and Biophysics·Verónica DemicheliRafael Radi
May 17, 2000·Biochimica Et Biophysica Acta·D Zaslavsky, R B Gennis
Jun 21, 2005·Archives of Biochemistry and Biophysics·Yeong-Renn ChenJay L Zweier
Oct 14, 2017·Chemical Reviews·Damián Alvarez-PaggiDaniel H Murgida

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