Cytochrome oxidase of an acidophilic iron-oxidizing bacterium, Thiobacillus ferrooxidans, functions at pH 3.5

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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.

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    The bacterium A. ferrooxidans AF3 was isolated from the Yufu mine of Hunan province in China (Chen et al. 2009). A. ferrooxidans was grown in 9K medium containing ferrous iron that was modified as described previously (Kai et al. 1989). Cultivation of A. ferrooxidans in high potassium concentration was carried out by adding KCl to 9K medium to a final concentration of 0.1 M.

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