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Catalytic and noncatalytic nucleotide binding sites of chloroplast F1 ATPase. Photoaffinity labeling and peptide sequencing
- Source :
- FEBS letters. 223(2)
- Publication Year :
- 1987
-
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.
- 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)
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 223
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- FEBS letters
- Accession number :
- edsair.doi.dedup.....ebe8ecf3faeb0ccf2c5fc40a7801278c