F1F0-ATP synthase: Development of direct optical probes of the catalytic mechanism

Joachim Weber, Alan E. Senior

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

Using strategically-placed tryptophan (Trp) residues as optical probes to monitor nucleotide binding and hydrolysis, we demonstrate that all three catalytic nucleotide binding sites in F1-ATPase must be filled to obtain physiological (V(max)) MgATP hydrolysis rates. At V,, hydrolysis rates, the predominant enzyme species has one of the three catalytic sites filled with unhydrolyzed substrate MgATP, the other two sites are filled with product MgADP. A specifically-inserted Trp probe was also developed to characterize nucleotide binding to the noncatalytic sites, and a model to explain the specificity of these sites is shown. These sites appear to play no role in ATP hydrolysis.

Original languageEnglish
Pages (from-to)101-104
Number of pages4
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1275
Issue number1-2
DOIs
StatePublished - Jul 18 1996

Keywords

  • ATP synthase
  • ATPase, F-
  • Catalytic mechanism
  • FF
  • Nucleotide binding site
  • Tryptophan fluorescence

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