Tunneling and Coupled Motion in the Escherichia coli Dihydrofolate Reductase Catalysis

  • R. Steven Sikorski
  • , Lin Wang
  • , Kelli A. Markham
  • , P. T.Ravi Rajagopalan
  • , Stephen J. Benkovic
  • , Amnon Kohen

Research output: Contribution to journalArticlepeer-review

Abstract

H-transfer was studied in the complex kinetic cascade of dihydrofolate reductase. Intrinsic kinetic isotope effects, their temperature dependence, and other temperature-dependent parameters indicated H-tunneling, but no 1° to 2° coupled motion. The data also suggested environmentally coupled tunneling and commitment to catalysis on pre-steady-state isotope effects.

Original languageEnglish (US)
Pages (from-to)4778-4779
Number of pages2
JournalJournal of the American Chemical Society
Volume126
Issue number15
DOIs
StatePublished - Apr 21 2004

All Science Journal Classification (ASJC) codes

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry

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