Enzymatic Mechanisms in the “Dehydrogenation” of Ferrous Ions by Thiobacillus Ferrooxidans (original) (raw)

Developments in Geochemistry, 1991

Abstract

Abstract From Thiobacillus ferrooxidans , an enzyme has been purified which catalyses oxidation of Fe 2+ ions with T. ferrooxidans cytochrome c -552 as the electron acceptor. The enzyme shows absorption peaks at 282 and 382 nm and contains 18-20 mol of nonhaem iron and 6 mol of inorganic sulphide in 63,000 g. The enzyme does not use rusticyanin as the electron acceptor for oxidation of Fe 2+ ions. T. ferrooxidans cytochrome c -552 has also been purified to an electrophoretically homogeneous state. It shows an absorption peak at 411 nm in the oxidized form and peaks at 417, 523 and 552 nm in the reduced form. Its molecular weight is about 14,000 and its redox potential at pH 7.0 is approx. +0.37 V.

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