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Inhibition of the ATPase activity of Escherichia coli ATP synthase by magnesium fluoride
Author(s) -
Ahmad Zulfiqar,
Senior Alan E.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.12.057
Subject(s) - atp synthase , atpase , escherichia coli , magnesium , chemistry , enzyme , biochemistry , mutant , fluoride , adenosine triphosphate , inorganic chemistry , gene , organic chemistry
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 ∼14 h at 22 °C and was quasi‐irreversible at 4 °C. Mutant F 1 ‐ATPases, in which catalytic site residues involved in transition state formation were modified, were found to be resistant to inhibition by MgFx. The data demonstrate that MgFx in combination with MgADP behaves as a tight‐binding transition state analog in E. coli ATP synthase.