A disulfide reductase in spores of Bacillus cereus T

Abstract

An enzyme obtained from Bacillus cereus T spores which catalyzes the reduction of the disulfide, 5, 5′-dithiobis (2-nitrobenzoic acid) (DTNB), has been partially purified and characterized. The enzyme required either reduced nicotinamide adenine dinucleotide phosphate (NADPH2) or reduced nicotinamide adenine dinucleotide (NADH2) as electron donor. It had a pH optimum of 8, was destroyed by heating at 70C for 5 min, and was stimulated by Ca2+ and Mg2+. No other small molecular weight disulfides were found to be substrates for the enzyme.