PMID:10727244
| Citation |
McLachlin, DT and Dunn, SD (2000) Disulfide linkage of the b and delta subunits does not affect the function of the Escherichia coli ATP synthase. Biochemistry 39:3486-90 |
|---|---|
| Abstract |
The ATP synthase of Escherichia coli is believed to act through a rotational mechanism in which the b(2)delta subcomplex holds the alphabeta hexamer stationary relative to the rotating gamma and epsilon subunits. We have engineered a disulfide bond between cysteines introduced at position 158 of the delta subunit and at a position just beyond the normal C-terminus of the b subunit. The formation of this disulfide bond verifies that the C-terminal region of b is proximal to residue 158 of delta. The disulfide bond does not affect the ability of the F(1)F(0) complex to hydrolyze ATP, couple ATP hydrolysis to the establishment of a proton gradient, or maintain a proton gradient generated by the electron transport chain. These results are consistent with a permanent association of b(2) with delta as suggested by the rotational model of enzyme function. |
| Links | |
| Keywords |
Adenosine Triphosphate/chemistry; Copper/chemistry; Cross-Linking Reagents/chemistry; Disulfides/chemistry; Escherichia coli/enzymology; Escherichia coli/genetics; Ethyldimethylaminopropyl Carbodiimide/chemistry; Hydrolysis; Mutagenesis, Site-Directed; Peptide Fragments/chemistry; Peptide Fragments/genetics; Polymerase Chain Reaction; Proton Pumps/chemistry; Proton-Translocating ATPases/chemistry; Proton-Translocating ATPases/genetics; Spectrometry, Fluorescence |
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