Purification and properties of hydrogen sulfide oxidase from Bacillus sp. BN53-1.
A hydrogen sulfide oxidase was purified to homogeneity from the heterotroph Bacillus sp. BN53-1 isolated from pig feces compost. The enzyme was found to be a monomer with a M(r) value of approximately 37 kDa. It required FAD for its activity, which was not replaced by FMN. The optimum reaction pH and temperature were 7.5 and 40 degrees C, respectively. The enzyme was stable between pH 6.0 and 7.0 and up to 30 degrees C. Its activity was stimulated by Ca2+ and Mn2+ and inhibited by Al3+, dithiothreitol, and 2-mercaptoethanol. The main product was elemental sulfur, and H2O2 was not detected. The N-terminal sequence of the enzyme showed similarity to other FAD-requiring enzymes.
Nakada
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Faculty of Applied Biological Science, Hiroshima University, 1-4-4 Kagamiyama, Higashi-Hiroshima 739-8528, Japan.
Ohta
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Y