Does F1-ATPase have a catalytic site that preferentially binds MgADP?

Hui Z. Mao, Wesley D. Gray, Joachim Weber

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


During ATP synthesis, ATP synthase has to bind MgADP in the presence of an excess of MgATP. Thus, for efficient ATP synthesis it would be desirable if incoming substrate could be bound to a catalytic site with a preference for MgADP over MgATP. We tested three hypotheses predicting the existence of such a site. However, our results showed that, at least in absence of an electrochemical proton gradient, none of the three catalytic sites has a higher affinity for MgADP than for MgATP.

Original languageEnglish
Pages (from-to)4131-4135
Number of pages5
JournalFEBS Letters
Issue number17
StatePublished - Jul 24 2006


  • ATP synthase
  • Binding change
  • Catalytic sites
  • Enzyme mechanism
  • F-ATPase
  • High-affinity site


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