Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

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

Hydrolysis and synthesis of ATP by membrane-bound ATPase from a motile Streptococcus 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Microbiology Springer Journals

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

Archives of Microbiology , Volume 119 (1) – Oct 1, 1978

Loading next page...
 
/lp/springer-journals/hydrolysis-and-synthesis-of-atp-by-membrane-bound-atpase-from-a-motile-4bryks3MFM

References (46)

Publisher
Springer Journals
Copyright
Copyright © 1978 by Springer-Verlag
Subject
Life Sciences; Biotechnology; Biochemistry, general; Cell Biology; Ecology; Microbial Ecology; Microbiology
ISSN
0302-8933
eISSN
1432-072X
DOI
10.1007/BF00407924
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Archives of MicrobiologySpringer Journals

Published: Oct 1, 1978

There are no references for this article.