ATP hydrolysis and synthesis by the membrane-bound ATP synthetase complex of Methanobacterium thermoautotrophicum | Zendy

Hans J. Doddema | Zendy; T. J. H. M. Hutten | Zendy; Chris van der Drift | Zendy; Godfried D. Vogels | Zendy

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ATP hydrolysis and synthesis by the membrane-bound ATP synthetase complex of Methanobacterium thermoautotrophicum

Author(s) -

Hans J. Doddema,

T. J. H. M. Hutten,

Chris van der Drift,

Godfried D. Vogels

Publication year - 1978

Publication title -

journal of bacteriology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.652

H-Index - 246

eISSN - 1067-8832

pISSN - 0021-9193

DOI - 10.1128/jb.136.1.19-23.1978

Subject(s) - chemiosmosis , atp hydrolysis , methanobacterium , biology , hydrolysis , atp synthase , thermophile , biochemistry , enzyme , anaerobic exercise , adenosine triphosphate , valinomycin , nucleoside , photophosphorylation , atpase , membrane , archaea , physiology , chloroplast , gene

The membrane-bound ATP synthetase complex of Methanobacterium thermoautotrophicum showed maximum activity for ATP hydrolysis at pH 8, at temperatures between 65 and 70 degrees C, and at an ATP-Mg2+ ratio of 0.5. Anaerobic conditions were not prerequisite for enzyme activity. The enzyme showed a Km value for ATP of 2 mM, and activity was Mg2+ dependent; Mn2+, Co2+, Ca2+, and Zn2+ could replace Mg2+ to some extent. Other nucleoside triphosphates could be hydrolyzed. N,N'-dicyclohexylcarbodiimide inhibited ATP hydrolysis. A proton-motive force, artificially imposed by a pH shift or valinomycin, resulted in ATP synthesis in whole cells. The ATP synthetase complex of the thermophilic methanogenic bacterium is similar to those described in aerobic and anaerobic microorganisms.

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