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Reversible effects of cross‐linking on the regulatory cooperativity of Acinetobacter citrate synthase
Author(s) -
Mitchell Colin G.,
Weitzman P.D.J.
Publication year - 1983
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(83)80082-9
Subject(s) - cooperativity , chemistry , citrate synthase , biochemistry , atp synthase , enzyme
Citrate synthase was purified from Acinetobacter calcoaceticus and treated with the cleavable cross‐linking reagent dithiobis(succinimidyl propionate). Cross‐linking of the enzyme resulted in the abolition of the sigmoidal responses to inhibition by NADH and re‐activation by AMP displayed by the native enzyme. Inhibition and re‐activation were still observed but without any cooperativity. Cleavage of the disulphide bonds in the cross‐links by treatment with dithiothreitol restored the sigmoidal characteristics of both inhibition and re‐activation.