F1-ATPase of Escherichia coli: The ε-inhibited State Forms After ATP Hydrolysis, is Distinct from the ADP-inhibited State, and Responds Dynamically to Catalytic-site Ligands

Shah, NB, et al., 288(13), 9383-95 , J Biol Chem, 2013

The authors use BLI experiments on the Octet RED system to study inhibition of E. coli F1-ATPase by its subunit ε. The binding and dissociation kinetics for F1-ε were determined and correlated with inhibitory effects for wild type and mutant forms of ε. Biotinylated ε species were loaded onto Streptavidin biosensors for these studies.

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