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• W2062370292 abstract "Under very mild oxidizing conditions the δ subunit of the F1-ATPase of Escherichia coli can be crosslinked by a disulfide linkage to one of the α subunits of the enzyme. The cross-linked ATPase resembles the native enzyme in the following properties: (1) specific activity; (2) activation by lauryldimethylamine N-oxide (LDAO); (3) binding of aurovertin D and ADP; (4) cross-linking products with 3,3′-dithiobis(succinimidyl propionate); (5) binding to ATPase-stripped everted membrane vesicles and the N,N′-dicyclohexylcarbodiimide sensitivity of the rebound enzyme. However, the rebound crosslinked ATPase differed from the native enzyme in lacking the ability to restore NADH oxidation - and ATP hydrolysis-dependent quenching of the fluorescence of quinacrine to ATPase-stripped membrane vesicles. It is proposed that the δ subunit is involved in the proton pathway of the ATPase, and that this pathway is affected in the αδ-cross-linked enzyme. The mechanism for activation of the ATPase by LDAO was examined. Evidence against the proposal of Lötscher, H.-R., De Jong, C. and Capaldi, R.A. (Biochemistry (1984) 23, 4140–4143) that activation involves displacement of the ε subunit from an active site on a β subunit was obtained." @default.
• W2062370292 created "2016-06-24" @default.
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• W2062370292 date "1986-10-01" @default.
• W2062370292 modified "2023-10-14" @default.
• W2062370292 title "Effect of disulfide cross-linking between α and δ subunits on the properties of the F1 adenosine triphosphatase of Escherichia coli" @default.
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• W2062370292 doi "https://doi.org/10.1016/0005-2728(86)90075-7" @default.
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