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Czarnecki JJ, Abbott MS, Selman BR. Photoaffinity labeling with 2-azidoadenosine diphosphate of a tight nucleotide binding site on chloroplast coupling factor 1. Proc Natl Acad Sci U S A. 1982;79(24):7744-8doi: 10.1073/pnas.79.24.7744.
Czarnecki, J. J., Abbott, M. S., & Selman, B. R. (1982). Photoaffinity labeling with 2-azidoadenosine diphosphate of a tight nucleotide binding site on chloroplast coupling factor 1. Proceedings of the National Academy of Sciences of the United States of America, 79(24), 7744-8. https://doi.org/10.1073/pnas.79.24.7744
Czarnecki, J J, et al. "Photoaffinity labeling with 2-azidoadenosine diphosphate of a tight nucleotide binding site on chloroplast coupling factor 1." Proceedings of the National Academy of Sciences of the United States of America vol. 79,24 (1982): 7744-8. doi: https://doi.org/10.1073/pnas.79.24.7744
Czarnecki JJ, Abbott MS, Selman BR. Photoaffinity labeling with 2-azidoadenosine diphosphate of a tight nucleotide binding site on chloroplast coupling factor 1. Proc Natl Acad Sci U S A. 1982 Dec;79(24):7744-8. doi: 10.1073/pnas.79.24.7744. PMID: 16593263; PMCID: PMC347424.
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Proc Natl Acad Sci U S A. 1982 Dec;79(24):7744-8. doi: 10.1073/pnas.79.24.7744.

Photoaffinity labeling with 2-azidoadenosine diphosphate of a tight nucleotide binding site on chloroplast coupling factor 1.

Proceedings of the National Academy of Sciences of the United States of America

J J Czarnecki, M S Abbott, B R Selman

Affiliations

  1. The Institute for Enzyme Research, College of Agricultural and Life Sciences, University of Wisconsin, Madison, Wisconsin 53706.

PMID: 16593263 PMCID: PMC347424 DOI: 10.1073/pnas.79.24.7744

Abstract

An analog of ADP containing an azido group at the C-2 position of the purine ring has been synthesized and used as an affinity probe of the membrane-bound coupling factor 1 of spinach chloroplast thylakoid membranes. The 2-azido-ADP inhibited light-induced dark binding of ADP at the tight nucleotide binding site on the thylakoid membranes. The 2-azido-ADP itself bound tightly to the thylakoid membranes, with 1 muM as the concentration giving 50% maximum binding. Tight binding of the analog required the thylakoid membranes to be energized, and the nucleotide remained bound after repeated washings of the membranes. The maximum extent of tight binding of the analog (1,2-1.3 nmol/mg of chlorophyll) was stoichiometric with the known coupling factor 1 content of thylakoid membranes but somewhat higher than that observed for ADP (0.5-0.9 nmol per mg of chlorophyll). Tight binding of 2-azido-ADP was decreased by the simultaneous addition of ADP. UV photolysis of washed thylakoid membranes containing tightly-bound 2-azido-[beta-(32)P]ADP resulted in the covalent incorporation of label into the membranes. Isolation of the chloroplast coupling factor 1 from these membranes followed by NaDodSO(4) gel electrophoresis demonstrated that the analog was covalently bound to the beta subunit of the coupling factor complex.

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