Features of F(1)-ATPase catalytic and noncatalytic sites revealed by fluorescence lifetimes and acrylamide quenching of specifically inserted tryptophan residues.

Abstract excerpt

Catalytic and noncatalytic nucleotide sites of the F(1) sector of ATP synthase were characterized by tryptophan fluorescence techniques. Seven Trp residues inserted in varied microenvironments in the catalytic sites, and one in the noncatalytic sites, were studied in mutant F(1) enzymes which were otherwise devoid of Trp. Parameters measured were fluorescence lifetimes and dynamic and static quenching by...

Topics

• Acrylamide
• Binding Sites
• Escherichia coli
• Kinetics
• Magnesium
• Models, Molecular
• Mutation
• Nucleotides
• Protein Binding
• Protein Conformation
• Proton-Translocating ATPases
• Spectrometry, Fluorescence
• Tryptophan