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. 1971 Dec;108(3):1112–1121. doi: 10.1128/jb.108.3.1112-1121.1971

Purification and Properties of Adenylyl Sulfate Reductase from the Phototrophic Sulfur Bacterium, Thiocapsa roseopersicina

Hans G Truper 1, Lynne A Rogers 1
PMCID: PMC247194  PMID: 5139533

Abstract

Adenylyl sulfate reductase was purified from Thiocapsa roseopersicina 60- to 80- fold, and the properties were studied. The molecular weight is 180,000. The enzyme contains, per molecule; one flavine group, two heme groups of cytochrome c character, four atoms of nonheme iron, and six labile sulfide groups. Cytochrome c and ferricyanide serve as electron acceptors. With ferricyanide as the electron acceptor, the pH optimum of the enzyme is at 8.0; with cytochrome c, the pH optimum is at 9.0. Of the nucleotides studied, adenosine 5′-monophosphate is most effective. The influence of substrate concentrations on the activity of the enzyme was studied, and the Km values for sulfite, adenosine 5′-monophosphate, ferricyanide, and cytochrome c were determined. The properties of the enzyme are compared with those of adenylyl sulfate reductases purified from sulfate-reducing bacteria and thiobacilli.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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