Glutathione reductase of Thiobacillus thio-oxidans

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Abstract
The presence of triphosphopyridine nucleotide-linked glutathione reductase was demonstrated in a cell-free extract of Thiobacillus thiooxidans. The pH optimum was found to be near 7.0. The activity was completely inhibited by 0.1 mM-p-chloromercuribenzoate and the inhibition was partially reversed by L-cysteine. The activity of an acid-treated extract was stimulated by flavinadenine dinucleotide, but not by riboflavin 5[image]-phosphate. Phosphate and, to a lesser extent, arsenate stimulated the enzymic action. A possible role of the enzyme in the oxidation of elemental S by the organism is discussed.

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