Structural asymmetry of the F1 of Escherichia coli as indicated by reaction with dicyclohexylcarbodiimide.
Dicyclohexylcarbodiimide (DCCD) inhibits the ATPase activity of F1 from Escherichia coli by covalent modification of a single glutamic acid in the beta subunit. 95% inhibition was obtained after incorporation of around 1 mole of DCCD per mole F1, i.e. 1 mole of reagent per 3 beta subunits; and up to 2 moles of DCCD per mole F1 were readily incorporated into the protein. One of the 3 beta subunits per F1 can be crosslinked to the epsilon subunit by 1-ethyl-3-[3(dimethylamino)propyl]carbodiimide (EDC). This beta subunit (beta 1) is here shown to be shielded from reaction with DCCD, presumably by its association with epsilon and also possibly the gamma subunit. Thus the three beta subunits are not equivalent in the enzyme complex.
D002234:Carbodiimides / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D003432:Cross-Linking Reagents; D004024:Dicyclohexylcarbodiimide / Q000378:metabolism* / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D011485:Protein Binding; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000378:metabolism
D002234:Carbodiimides; D003432:Cross-Linking Reagents; D004024:Dicyclohexylcarbodiimide; D006180:Proton-Translocating ATPases