Cooperativity and stoichiometry of substrate binding to the catalytic sites of Escherichia coli F1-ATPase. Effects of magnesium, inhibitors, and mutation.

Article

Cooperativity and stoichiometry of substrate binding to the catalytic sites of Escherichia coli F1-ATPase. Effects of magnesium, inhibitors, and mutation.

The Journal of biological chemistry - 12 Aug 1994

Weber J, Wilke-Mounts S, Senior A E

Abstract excerpt

The fluorescence of residue Trp beta 331 in beta Y331W mutant Escherichia coli F1-ATPase was used as reporter probe to investigate the effects of magnesium ions, inhibitors, and mutation on substrate (ATP) binding stoichiometry and cooperativity. It was found that Mg2+ is required for catalytic s...

Topics

Adenosine Triphosphate
Catalysis
Dicyclohexylcarbodiimide
Escherichia coli
Ethylmaleimide
Magnesium
Mutation
Proton-Translocating ATPases
Substrate Specificity

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