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.
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Abbreviations
- \(\Delta \mu _{{\text{H}}^{\text{ + }} } \) :
-
electrochemical gradient of protons
- DMO:
-
5,5-dimethyl-2,4-oxazolidinedione
- CCCP:
-
carbonylcyanide m-chlorophenylhydrazone
- FCCP:
-
carbonylcyanide p-trifluoromethoxyphenylhydrazone
- DCCD:
-
N,N′-dicyclohexylcarbodiimide
- DNP:
-
2,4-dimitrophenol
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van der Drift, C., Janssen, D.B. & van Wezenbeek, P.M.G.F. Hydrolysis and synthesis of ATP by membrane-bound ATPase from a motile Streptococcus . Arch. Microbiol. 119, 31–36 (1978). https://doi.org/10.1007/BF00407924
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DOI: https://doi.org/10.1007/BF00407924