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Direct identification of the fluoroaluminate and fluoroberyllate species responsible for inhibition of the mitochondrial F 1 ‐ATPase
Author(s) -
Dupuis Alain,
Issartel Jean-Paul,
Vignais Pierre V.
Publication year - 1989
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 - 10.1016/0014-5793(89)81058-0
Subject(s) - beryllium , stoichiometry , atpase , fluoride , chemistry , enzyme , mole , sodium fluoride , inorganic chemistry , stereochemistry , biochemistry , organic chemistry
In the presence of ADP, fluoroaluminate and fluoroberyllate inhibit irreversibly the soluble mitochondrial F 1 ‐ATPase. We report here direct evidence that this inhibition is related to the tight binding of [ 3 H]ADP, beryllium and fluoride to the enzyme. In the case of beryllium‐induced inhibition, the stoichiometry of bound species is 1 mol [ 3 H]ADP, 1 mol beryllium and 2 or 3 mol fluoride depending on the initial fluoride concentration used, which indicates that both the combinations ADP 1 ,Be 1 ,F 3 and ADP 1 ,Be 1 ,F 3 are competent for inhibition. In the case of aluminium‐induced inhibition, the binding stoichiometry of 4 mol fluoride per mol [ 3 H]ADP favours the following combination of bound species ADP 1 ,Al 1 ,F 4 . These results favour a model where fluorometals mimic phosphate and form an abortive complex with ADP in the catalytic site(s) of F 1 .