Interaction of beef-heart mitochondrial ATPase, coupling factor F1, with aurovertin.
The antibiotic aurovertin binds to beef-heart mitochondrial ATPase, coupling Factor F1, with biphasic fluorescence enhancement. Specific binding effects, polarity and viscosity changes may all contribute to the enhancement. Evidence is presented that it stems from aurovertin binding followed by a slow conformational change in F1. This occurs more rapidly in dissociated F1. The effect of substrates of the enzyme on the fluorescence enhancement is examined. Evidence is presented that in the absence of added magnesium, F1 can hydrolyse low concentrations of added ATP.
Yeates
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Laboratory of Biochemistry, B. C. P. Jansen Institute, University of Amsterdam, Amsterdam, The Netherlands.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001313:Aurovertins / Q000378:metabolism*; D002417:Cattle; D008929:Mitochondria, Heart / Q000201:enzymology*; D025261:Mitochondrial Proton-Translocating ATPases / Q000378:metabolism*; D014475:Uncoupling Agents / Q000378:metabolism*
D001313:Aurovertins; D014475:Uncoupling Agents; D000255:Adenosine Triphosphate; D025261:Mitochondrial Proton-Translocating ATPases