Affiliation:
1. Department of Biochemistry, University of Georgia, Athens, Georgia 30601
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 m
m
, and activity was insensitive to inhibition by ouabain. The ATPase was stimulated by both Ca
2+
and Mg
2+
, but the magnitude of the stimulation was dependent upon
p
H. In the presence of Ca
2+
the optimum
p
H was 6.5, whereas, in the presence of Mg
2+
the
p
H optimum was 8.0. However, under optimal conditions the activity was the same with either Mg
2+
or Ca
2+
. Both adenosine triphosphate and guanosine triphosphate were hydrolyzed, but activity toward guanosine triphosphate was only one-tenth that observed with adenosine triphosphate.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
33 articles.
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