Quantum-classical simulation methods for hydrogen transfer in enzymes: A case study of dihydrofolate reductase

Sharon Hammes-Schiffer

Research output: Contribution to journalReview articlepeer-review

Abstract

A variety of theoretical approaches have been used to investigate hydrogen transfer in enzymatic reactions. The free energy barriers for hydrogen transfer in enzymes have been calculated using classical molecular dynamics simulations in conjunction with quantum mechanical/molecular mechanical and empirical valence bond potentials. Nuclear quantum effects have been included with several different approaches. Applications of these approaches to hydride transfer in dihydrofolate reductase are consistent with experimental measurements and provide significant insight into the protein conformational changes that facilitate the hydride transfer reaction.

Original languageEnglish (US)
Pages (from-to)192-201
Number of pages10
JournalCurrent Opinion in Structural Biology
Volume14
Issue number2
DOIs
StatePublished - Apr 1 2004

Keywords

  • DHF
  • DHFR
  • Dihydrofolate
  • Dihydrofolate reductase
  • EVB
  • Empirical valence bond
  • KIE
  • Kinetic isotope effect
  • MM
  • MOVB
  • Molecular mechanical
  • Molecular orbital-valence bond
  • NADPH
  • Nicotinamide adenine dinucleotide phosphate
  • QM
  • Quantum mechanical
  • THF

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Quantum-classical simulation methods for hydrogen transfer in enzymes: A case study of dihydrofolate reductase'. Together they form a unique fingerprint.

Cite this