1. Catalytic and noncatalytic nucleotide binding sites of chloroplast F1 ATPase. Photoaffinity labeling and peptide sequencing
- Author
-
Jun-Mei Zhou, Chad G. Miller, Zhixiong Xue, and Paul D. Boyer
- Subjects
Chloroplasts ,Photochemistry ,ATPase ,Biophysics ,Biochemistry ,Peptide Mapping ,Adenosine Triphosphate ,Structural Biology ,Peptide sequence ,Genetics ,Moiety ,2-Azido-ATP ,Nucleotide ,Binding site ,Tyrosine ,Molecular Biology ,chemistry.chemical_classification ,Binding Sites ,biology ,Photoaffinity labeling ,Chemistry ,Adenine Nucleotides ,Site labeling ,Affinity Labels ,Cell Biology ,Peptide Fragments ,Adenosine Diphosphate ,Proton-Translocating ATPases ,Enzyme ,biology.protein ,F1 ATPase ,(Chloroplast) - Abstract
Exposure of chloroplast F1 ATPase to 2-azido-ATP results in the noncovalent tight binding of 2-azido-ATP or 2-azido-ADP to noncatalytic or to catalytic sites. Subsequent photolysis results in covalent labeling of adjacent tryptic peptides of the β-subunit. Binding at noncatalytic sites results in labeling of tyrosine 385 by an ATP or an ADP moiety. Binding at catalytic sites results in labeling of tyrosine 362 by only an ADP moiety. Similar labeling patterns are observed for the heat-activated or the membrane-bound enzymes.
- Published
- 1987