Selective Reduction of Cytochrome c Oxidase with Borohydride
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چکیده
منابع مشابه
Selective Reduction of Cytochrome C Oxidase with Borohydride.
Since the pioneer studies of Keilin and Hartree (l), considerable evidence has accumulated indicating that cytochrome c oxidase contains two heme moieties that react differently; hence the designation cytochrome U-Q. Reasons for this designat.ion include kinetic studies that show (a) differences in the rate of reduction and oxidation of cytochrome c oxidase measured at the a versus y absorption...
متن کاملTHE REDUCTION OF CYTOCHROME c BY XANTHINE OXIDASE
A number of substances such as oxygen, dyes, and nitrate can act as hydrogen acceptors for xanthine oxidase (1). It has now been found that cytochrome c is also reduced by this system. Since only one other enzyme has been isolated which reduces cytochrome c (2), it was of interest to study the reaction, particularly since Ball (3) has indicated that xanthine oxidase is a flavoprotein. The activ...
متن کاملThe reduction of cytochrome c by milk xanthine oxidase.
The reduction of cytochrome c by xanthine oxidase and the competitive inhibition of this process by carbonic anhydrase and by myoglobin have been studied by kinetic and by equilibrium binding methods. Carbonic anhydrases isolated from bovine and from human erythrocytes differed strikingly in their ability to inhibit competitively the reduction of cytochrome c. The KS for cytochrome c was a func...
متن کاملThe reduction of cytochrome c by hypoxanthine and xanthine oxidase.
Ball, E. G. (1939a). J. biol. Chem. 128, 51. Ball, E. G. (1939b). Cold Spr. Harb. Sym. quant. Biol. 7, 100. Ball, E. G. (1946). J. gen. Phy8iol. 29, 413. Corran, H. S., Dewan, J. G., Gordon, A. H. & Green, D. E. (1939). Biochem. J. 38, 1694. Dixon, M. (1938). Enzymologia, 5, 198. Dixon, M. & Keilin, D. (1936). Proc. roy. Soc. B, 119, 159. Green, D. E., Knox, W. E. & Stumpf, P. K. (1941). J. bio...
متن کاملAssembly of cytochrome c oxidase: what can we learn from patients with cytochrome c oxidase deficiency?
Cytochrome c oxidase is an intricate metalloprotein that transfers electrons from cytochrome c to oxygen in the last step of the mitochondrial respiratory chain. It uses the free energy of this reaction to sustain a transmembrane electrochemical gradient of protons. Site-directed mutagenesis studies of bacterial terminal oxidases and the recent availability of refined crystal structures of the ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1965
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)97590-3