Purification and some properties of sulfur:ferric ion oxidoreductase from Thiobacillus ferrooxidans.

作者: T Sugio , W Mizunashi , K Inagaki , T Tano

DOI: 10.1128/JB.169.11.4916-4922.1987

关键词:

摘要: Sulfite:ferric ion oxidoreductase in the plasma membrane of Thiobacillus ferrooxidans AP19-3 was purified to an electrophoretically homogeneous state. The enzyme had apparent molecular weight 650,000 and composed two subunits (M(rs), 61,000 59,000) as estimated by sodium sulfate-polyacrylamide gel electrophoresis. Michaelis constants sulfite:ferric for Fe3+ sulfite ions were 1.0 0.071 mM, respectively. suffered from end product inhibition 1 mM Fe2+.

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