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Structural and functional modifications induced by diamide on the F 0 sector of the mammalian ATP synthase
Author(s) -
Dabbeni-Sala Federica,
Lippe Giovanna,
Sorgato M.Catia
Publication year - 1991
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(91)80355-7
Subject(s) - atp synthase , protein subunit , cysteine , dimer , chemistry , reagent , thiol , enzyme , biochemistry , atp synthase gamma subunit , proton , stereochemistry , biophysics , atp hydrolysis , biology , atpase , organic chemistry , physics , quantum mechanics , gene
In this report data are presented which firmly establish that by treating isolated F 0 with the thiol reagent diamide, two 25 kDa F 0 subunits react to form a dimer of 45 kDa apparent molecular mass. This dimerising effect is correlated to the impairment of the binding of F 1 to F 0 , both at μM and mM diamide concentrations. Under the latter condition, modification of other F 0 subunits also occurs. Passive proton conductance through F 0 , as well as its sensitivity to N , N ′‐dicyclohexylcarbodiimide, are affected at low diamide concentration. Thus perturbation of the cysteine residue of the 25 kDd F 0 subunit is sufficient for altering the ATP synthase proton channel.