Inhibition of the ATPase activity of Escherichia coli ATP synthase by magnesium fluoride.

doi:10.1016/j.febslet.2005.12.057

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Article

Inhibition of the ATPase activity of Escherichia coli ATP synthase by magnesium fluoride.

FEBS letters - 23 Jan 2006

Ahmad Zulfiqar, Senior Alan E

Abstract excerpt

Inhibition of ATPase activity of Escherichia coli ATP synthase by magnesium fluoride (MgFx) was studied. Wild-type F(1)-ATPase was inhibited potently, albeit slowly, when incubated with MgCl(2), NaF, and NaADP. The combination of all three components was required. Reactivation of ATPase activity, after removal of unbound ligands, occurred with half-time of approximately 14 h at 22 degrees C and was...

Topics

Adenosine Diphosphate
Animals
Catalytic Domain
Enzyme Activation
Escherichia coli
Escherichia coli Proteins
Fluorides
Ligands
Magnesium Chloride
Magnesium Compounds
Mutation
Proton-Translocating ATPases

Source

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Identifiers

PMID: 16405964
DOI: 10.1016/j.febslet.2005.12.057

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