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PMID: 31147 Published · ppublish English Journal Article

Hydrolysis and synthesis of ATP by membrane-bound ATPase from a motile Streptococcus.

Archives of microbiology ·Vol. 119 ·No. 1 ·1978-10-04 ·Pages 31-6

van der Drift C, Janssen DB, van Wezenbeek PM

Abstract

ATPase was detected in the membranes of a motile Streptococcus. Maximal enzymic activity was observed at pH 8 and ATP/Mg2+ ratio of 2. Mn2+ and Ca2+ could replace Mg2+ to some extent. Besides ATP, GTP and ITP were substrates. The enzyme was inhibited by N,N'-dicyclohexylcarbodiimide but not by sodium azide, uncouplers or bathophenanthroline. An electrochemical gradient of protons, which was artificially imposed across the membranes of Streptococcus cells by manipulation of either the K+ diffusion potential or the transmembrane pH gradient, led to ATP synthesis. ATP synthesis was abolished by proton conductors, an inhibitor of the ATPase or an increase in the extracellular K+ concentration. A comparison between the phosphate potential and the electrochemical proton gradient showed that the data found are in agreement with a stoichiometry of 2 protons translocated per molecule ATP synthesized.

MeSH Terms
Adenosine Triphosphatases/metabolism Adenosine Triphosphate/biosynthesis,metabolism Cell Membrane/physiology Hydrogen-Ion Concentration Hydrolysis Membrane Potentials Movement Streptococcus/metabolism,physiology Uncoupling Agents/pharmacology Valinomycin/pharmacology
Chemicals
Uncoupling Agents Valinomycin Adenosine Triphosphate Adenosine Triphosphatases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
van der Drift C
Janssen D B
van Wezenbeek P M
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33 references, click to expand
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Article Info
Journal
Archives of microbiology
Abbr.
Arch Microbiol
ISSN
0302-8933
DOI
10.1007/BF00407924
Published
1978-10-04
Pages
31-6
Language
English
Region
Germany
NLM ID
0410427
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00407924 View journal details
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