Molybdenum oxidation by Thiobacillus ferrooxidans

Article Abstract:

Molybdenum blue was oxidized enzymatically by aerobically growing cells of Thiobacillus ferrooxidans AP19-3. The enzyme, molybdenum oxidase, was located in the plasma membrane. The purified enzyme had an optimum pH of 5.5, and was inhibited by 4.0 mM molybdenum blue as well as by sodium cyanide and carbon monoxide. The enzyme also contained cytochrome oxidase as shown by its two absorption maxima and ability to reduce mammalian cytochrome c. Results also indicated that the cytochrome oxidase may also play a crucial role in molybdenum oxidation.

Observations, Oxidases

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Isolation and characterization of a Mo6+-reducing bacterium

Article Abstract:

A bacterium capable of reducing molybdenum was derived from a Malaysian stream and isolated by incubation. The determination of the amount of molybdenum blue formed by the bacterium enabled the characterization of molybdenum reductase activity. The biuret method was used to determine protein content. The capability of the heterotrophic bacterium for molybdenum reduction was established.

Research, Bacteria

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Ferrous iron-dependent volatilization of mercuty by the plasma membrane of Thiobacillus ferrooxidans

Article Abstract:

Results demonstrate that plasma membrane of Thiobacillus ferrooxidans SUG 2-2 can volatilize mercury from salt solutions containing ferrous iron even in the absence of NADPH-dependent mercury reductase activity. Data also indicate that the mercury volatilization activity is promoted by the copper protein rusticyanin.

United States, Japan, Statistical Data Included, Bacterial cell walls, Cell membranes, Plasma membranes, Mercury, Mercury (Metal)

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