Article
ATP hydrolysis-driven structural changes in the gamma-subunit of Escherichia coli ATPase monitored by fluorescence from probes bound at introduced cysteine residues.
The Journal of biological chemistry - 6 May 1994
Turina P, Capaldi R A
Abstract excerpt
Four mutants of the Escherichia coli F1ATPase, gamma S8-C, gamma T106-C, gamma S179-C, and gamma V286-C, which have a cysteine introduced at different sites in the gamma-subunit by site-directed mutagenesis, were reacted with the fluorescent reagent N-(4-7-(diethylamino)4-methylcoumarin-3-yl)-mal...
Topics
- Adenosine Triphosphate
- Coumarins
- Cysteine
- Escherichia coli
- Fluorescence Polarization
- Fluorescent Dyes
- Hydrolysis
- Kinetics
- Maleimides
- Mutation
- Nucleotides
- Protein Conformation
- Proton-Translocating ATPases