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203 119 119 1 1 C. van der Drift D. B. Janssen P. M. G. F. van Wezenbeek Department of Microbiology, Faculty of Science University of Nijmegen Nijmegen The Netherlands Abstract ATPase was detected in the membranes of a motile Streptococcus . Maximal enzymic activity was observed at pH 8 and ATP/Mg 2+ ratio of 2. Mn 2+ and Ca 2+ could replace Mg 2+ 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.
Archives of Microbiology – Springer Journals
Published: Oct 1, 1978
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