New biophysical probes for structure-activity analyses of vacuolar-H +-ATPase enzymes

Neil Dixon, Tibor Pali, Stephen Ball, Michael A. Harrison, Derek Marsh, John B.C. Findlay, Terence P. Kee

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The structure and synthesis of the vacuolar H+-ATPase enzymes were studied. Two latest molecular probes, including the electron spin labels and photoactivable labels, were used for the analysis of inhibitor binding to the vacuolar ATPase enzyme. The electron paramagnetic resonance (EPR) spectroscopy studies indicated the incorporation of the inhibitors within membranes. On the other hand, the photoaffinity labeling (PAL) investigation suggested that the members of the V-ATPase inhibitors targeted the transmembrane, proteolipid component of the enzyme.

Original languageEnglish
Pages (from-to)4361-4363
Number of pages3
JournalOrganic and Biomolecular Chemistry
Volume1
Issue number24
DOIs
Publication statusPublished - Dec 21 2003

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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    Dixon, N., Pali, T., Ball, S., Harrison, M. A., Marsh, D., Findlay, J. B. C., & Kee, T. P. (2003). New biophysical probes for structure-activity analyses of vacuolar-H +-ATPase enzymes. Organic and Biomolecular Chemistry, 1(24), 4361-4363. https://doi.org/10.1039/b311401e