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PMID: 134890 Published · ppublish English Journal Article

Localization and possible role of an adenosine triphosphatase in Chlorobium thiosulfatophilum.

European journal of biochemistry ·Vol. 67 ·No. 2 ·1976-08-16 ·Pages 323-33

Burns DD, Midgley M

Abstract

1. Evidence is presented that the ATPase activity detected in cell extracts of Chlorobium thiosulfatophilum is bound to the cytoplasmic membrane rather than to the chlorobium vesicles. 2. The activity of this ATPase is inhibited in vitro by various carbodiimides, phloridzin and sodium azide. 3. The apparent Km for ATP is approximately 0.2 mM and the enzyme shows product inhibition by ADP. 4. Photophosphorylation, characterized in vivo, is inhibited by many of the compounds that inhibit the ATPase.

MeSH Terms
Adenosine Diphosphate/pharmacology Adenosine Triphosphatases/metabolism Adenosine Triphosphate/metabolism Bacteria/drug effects,enzymology Carbodiimides/pharmacology Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology Cell Membrane/enzymology Dinitrophenols/pharmacology Electron Transport Kinetics Light Photophosphorylation/drug effects Quinolines/pharmacology Subcellular Fractions/enzymology
Chemicals
Carbodiimides Dinitrophenols Quinolines Carbonyl Cyanide m-Chlorophenyl Hydrazone Adenosine Diphosphate Adenosine Triphosphate Adenosine Triphosphatases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Burns D D
Midgley M
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1976-08-16
Pages
323-33
Language
English
Region
England
NLM ID
0107600
Subset
IM
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