Purification and Characterization of Sulfur Reductase from a Moderately Thermophilic Bacterical Strain, TI-1,that Oxidizes Iron

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A moderately thermophilic bacterium, strain TI-1,produces H_2S outside of the cells when grown at 45℃ on Fe^<2+> -medium (pH 1.8) containing elemental sulfur and L-glutamic acid. A newly identified sulfur reductase was present in the cytosol of this strain and was purified to an electrophoretically homogeneous state from strain TI-1. The apparent molecular weight of sulfur reductase was 86,000 by gel filtration and 48,000 by SDS-PAGE, so the enzyme was a homodimer. The enzyme was most active at pH 9.0 and 60 to 70℃, and it catalyzed reduction of 1 mol of elemental sulfur with 1 mol of NADH to give 1 mol of H_2S and 1 mol of NAD^+. Elemental sulfur was a specific electron acceptor of this enzyme. Thiosulfate, sulfite, and tetrathionate were not electrom acceptors, but inhibited sulfur reductase activity. NADPH was not used as an electron donor.
社団法人日本農芸化学会の論文
1998-04-23