FEBS Letters | |
Catalytic and noncatalytic nucleotide binding sites of the Escherichia coli F1 ATPase Amino acid sequences of β‐subunit tryptic peptides labeled with 2‐azido‐ATP | |
Wise, John G.1  Boyer, Paul D.1  Hicke, Brian J.1  | |
[1] Department of Chemistry and Biochemistry and Molecular Biology Institute, University of California, Los Angeles, CA 90024-1570, USA | |
关键词: H+-ATPase; Oxidative phosphorylation; Photoaffinity analog; Azido-ATP; (E. coli); | |
DOI : 10.1016/0014-5793(87)80326-5 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Under appropriate conditions tight, noncovalent binding of 2-azido-adenine nucleotides to either catalytic or noncatalytic binding sites on the E. coli F1-ATPase occurs. After removal of unbound ligands, UV-irradiation results primarily in the covalent incorporation of nucleotide moieties into the β-subunit in both catalytic and noncatalytic site labeling experiments. Minor labeling of the α-subunit was also observed. After trypsin digestion and purification of the labeled peptides, microsequencing studies identified two adjacent β-subunit tryptic peptides labeled by 2-azido-ADP or -ATP. These β-subunit peptides were labeled on tyrosine-331 (catalytic sites) and tyrosine-354 (noncatalytic sites) in homology with the labeling patterns of the mitochondrial and chloroplast enzymes.
【 授权许可】
Unknown
【 预 览 】
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