Isolation of a Bisulfite Reductase Activity from Desulfotomaculum nigrificans and Its Identification as the Carbon Monoxide-Binding Pigment P582

Author:

Akagi J. M.1,Adams Verna1

Affiliation:

1. Department of Microbiology, University of Kansas, Lawrence, Kansas 66045

Abstract

Crude preparations of Desulfotomaculum nigrificans were found to reduce bisulfite to trithionate, thiosulfate, and sulfide. The bisulfite reductase of this organism was partially purified and observed to reduce bisulfite to trithionate as the major product and with thiosulfate and sulfide as minor products. The enzyme exhibited spectral properties identical to the carbon monoxide-reacting pigment (P582) isolated from this organism. It is concluded that the bisulfite reductase of D. nigrificans is P582 and that this organism utilizes a pathway which involves trithionate during the reduction of bisulfite to sulfide.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference14 articles.

1. Spectrophotometric determination of hydrogen sulfide;Fogo J. K.;Anal. Chem.,1949

2. Cyanolysis and spectrophotometric estimation of trithionate in mixture with thiosulfate and tetrathionate;Kelly D. P.;Anal. Chem.,1969

3. Intermediary formation of trithionate in sulfite reduction by a sulfate-reducing bacterium;Kobayashi K.;J. Biochem. (Tokyo),1969

4. Biochemical studies on sulfate-reducing bacteria XI. Purification and some properties of sulfite reductase, desulfoviridin;Kobayashi K.;J. Biochem. (Tokyo),1972

5. Purification of the enzyme reducing bisulfite to trithionate from Desulfovibrio gigas and its identification as desulfoviridin;Lee J. P.;Biochem. Biophys. Res. Commun.,1971

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