Relating protein motion to catalysis

Sharon Hammes-Schiffer, Stephen J. Benkovic

Research output: Contribution to journalReview articlepeer-review

513 Scopus citations


This review examines the linkage between protein conformational motions and enzyme catalysis. The fundamental issues related to this linkage are probed in the context of two enzymes that catalyze hydride transfer, namely dihydrofolate reductase and liver alcohol dehydogenase. The extensive experimental and theoretical studies addressing the role of protein conformational changes in these enzyme reactions are summarized. Evidence is presented for a network of coupled motions throughout the protein fold that facilitate the chemical reaction. This network is comprised of fast thermal motions that are in equilibrium as the reaction progresses along the reaction coordinate and that lead to slower equilibrium conformational changes conducive to the chemical reaction.

Original languageEnglish (US)
Pages (from-to)519-541
Number of pages23
JournalAnnual review of biochemistry
StatePublished - 2006
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry


  • Dihydrofolate reductase
  • Enzyme catalysis
  • Liver alcohol dehydrogenase
  • Protein conformational motions


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