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Catalytic and noncatalytic nucleotide binding sites of chloroplast F 1 ATPase Photoaffinity labeling and peptide sequencing
Author(s) -
Xue Zhixiong,
Miller Chad G.,
Zhou Jun-Mei,
Boyer Paul D.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80325-3
Subject(s) - photoaffinity labeling , moiety , chloroplast , chemistry , biochemistry , atpase , tyrosine , nucleotide , affinity label , covalent bond , peptide , binding site , diazirine , affinity labeling , protein subunit , enzyme , stereochemistry , organic chemistry , gene
Exposure of chloroplast F 1 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.