| Literature DB >> 2541715 |
M Kai1, T Yano, Y Fukumori, T Yamanaka.
Abstract
Cytochrome oxidase of Thiobacillus ferrooxidans was partially purified. The oxidase preparation had haems a and c, and oxidized ferrocytochrome c-552 of the bacterium. The optimal pH of the reaction was 3.5. The enzyme also oxidized the reduced form of rusticyanin, a copper protein of the bacterium. Our results indicate that the reduction of molecular oxygen by this enzyme may occur in the periplasm.Entities:
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Year: 1989 PMID: 2541715 DOI: 10.1016/0006-291x(89)92510-2
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575