Purification and Properties of Sulfite Reductase from Desulfovibrio vulgaris, Miyazaki F

抄録

The sulfite reductase of Desulfovibrio vulgaris, strain Miyazaki F (MF), was purified by ammonium sulfate precipitation and chromatography on DEAE-cellulose, Ultrogel AcA34, and hydroxylapatite. The molecular weight was estimated to be 180, 000 by gel filtration. It had a subunit structure of α₂β₂; the molecular weight of the α subunit was 50, 000 and that of β, 39, 000. The absorption spectrum with characteristic peaks at 629 and 409 nm and the amino acid composition resembled those of the sulfite reductase from D. vulgaris, Miyazaki K. The MF enzyme reduced sulfite to trithionate, thiosulfate, and sulfide by hydrogen when coupled with a hy-drogenase-methyl viologen system, like other sulfite reductases from Desulfovibrio.