TELLURITE REDUCTASE FROM MYCOBACTERIUM AVIUM

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Abstract
A cell-free extract of M. avium capable of reducing tellurite was obtained, and tellurite-reducing enzyme, referred to as tellurite reductase, was separated from malic dehydrogenase in the soluble fraction. The electron donor of this reduction was malate in the presence of L-malic dehydrogenase in soluble fraction, which could be replacedby reduced diphosphopyridine nucleotide. The optimum pH of this reductase was 6.5. The supernatant fluid of boiled soluble fraction and ferrous or ferric ion were required for the maximal reduction of tellurite by the reductase.