A perspective on biological catalysis

William R. Cannon, Scott F. Singleton, Stephen Benkovic

Research output: Contribution to journalReview articlepeer-review

127 Scopus citations

Abstract

We have analysed enzyme catalysis through a re-examination of the reaction coordinate. The ground state of the enzyme-substrate complex is shown to be related to the transition state through the mean force acting along the reaction path; as such, catalytic strategies cannot be resolved into ground state destabilization versus transition state stabilization. We compare the role of active-site residues in the chemical step with the analogous role played by solvent molecules in the environment of the noncatalysed reaction. We conclude that enzyme catalysis is significantly enhanced by the ability of the enzyme to preorganize the reaction environment. This complementation of the enzyme to the substrate's transition state geometry acts to eliminate the slow components of solvent reorganization required for reactions in aqueous solution. Dramatically strong binding of the transition state geometry is not required.

Original languageEnglish (US)
Pages (from-to)821-833
Number of pages13
JournalNature Structural Biology
Volume3
Issue number10
DOIs
StatePublished - Oct 1 1996

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Genetics

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