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. 1971 Jun;106(3):890–895. doi: 10.1128/jb.106.3.890-895.1971

Dinitrophenol-Stimulated Adenosine Triphosphatase Activity in Extracts of Desulfovibrio gigas1

Leonard J Guarraia a,2, Harry D Peck Jr a
PMCID: PMC248717  PMID: 4254119

Abstract

A dinitrophenol (DNP)-stimulated adenosine triphosphatase (ATPase) has been found in both the soluble and particulate fractions of the anaerobic sulfate-reducing bacterium, Desulfovibrio gigas. As the soluble ATPase was labile to storage, only the particulate enzyme was studied in detail. It was optimally stimulated by DNP at 4 mm, and activity was insensitive to inhibition by ouabain. The ATPase was stimulated by both Ca2+ and Mg2+, but the magnitude of the stimulation was dependent upon pH. In the presence of Ca2+ the optimum pH was 6.5, whereas, in the presence of Mg2+ the pH optimum was 8.0. However, under optimal conditions the activity was the same with either Mg2+ or Ca2+. Both adenosine triphosphate and guanosine triphosphate were hydrolyzed, but activity toward guanosine triphosphate was only one-tenth that observed with adenosine triphosphate.

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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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