F1F0-ATP synthase: development of direct optical probes of the catalytic mechanism.

Abstract

Using strategically-placed tryptophan (Trp) residues as optical probes to monitor nucleotide binding and hydrolysis, we demonstrate that all three catalytic nucleotide binding sites in F1-ATPase must be filled to obtain physiological (Vmax) MgATP hydrolysis rates. At Vmax hydrolysis rates, the predominant enzyme species has one of the three catalytic sites… (More)

Topics

Cite this paper

@article{Weber1996F1F0ATPSD, title={F1F0-ATP synthase: development of direct optical probes of the catalytic mechanism.}, author={Jessica L. Weber and Alan E. Senior}, journal={Biochimica et biophysica acta}, year={1996}, volume={1275 1-2}, pages={101-4} }