Catalytic and noncatalytic nucleotide binding sites of chloroplast F1 ATPase Photoaffinity labeling and peptide sequencing

FEBS Letters

Boyer, Paul D.¹  Xue, Zhixiong¹  Miller, Chad G.¹  Zhou, Jun-Mei¹ 

[1] Department of Chemistry and Biochemistry and Molecular Biology Institute, University of California, Los Angeles, CA, 90024-1570, USA

关键词: 2-Azido-ATP;    F1 ATPase;    Site labeling;    Peptide sequence;    (Chloroplast);   

DOI  :  10.1016/0014-5793(87)80325-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown