Chromatium sulfite reductase. I. Characterization of thiosulfate-forming activity at the cell extract level.
Thiosulfate and sulfide were detected in the sulfite reductase reaction catalyzed by a cell-free extract of photoautotrophically grown Chromatium vinosum. Hydrogen was consumed upon addition of sulfite to the extract in the presence of hydrogenase and methylviologen. Hydrogen uptake proceeded biphasically. During the first phase, thiosulfate and sulfide were formed concomitant with the decrease in sulfite. After the disappearance of sulfite, hydrogen was consumed with reduced velocity and sulfide accumulated as the final product with the total consumption of three mol of hydrogen per mol of sulfite. The molecular weight of a major sulfite reductase was estimated to be about 180,000 by the polyacrylamide disc electrophoresis method using enzyme staining. Arsenite. EDTA, alpha,alpha'-dipyridyl, cyanide, or azide did not inhibit the activity at the concentration of 1 mM. The activity was present in the soluble fraction and was stable at --20 degrees C.
D015082:2,2'-Dipyridyl / Q000494:pharmacology; D002844:Chromatium / Q000201:enzymology*; D006859:Hydrogen / Q000378:metabolism; D010088:Oxidoreductases / Q000378:metabolism*; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000378:metabolism*; D010269:Paraquat / Q000378:metabolism; D013347:Subcellular Fractions / Q000201:enzymology; D013447:Sulfites / Q000378:metabolism; D013885:Thiosulfates / Q000378:metabolism*
D013447:Sulfites; D013885:Thiosulfates; D015082:2,2'-Dipyridyl; D006859:Hydrogen; D010088:Oxidoreductases; D050862:Oxidoreductases Acting on Sulfur Group Donors; D010269:Paraquat