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Keywords:

  • deuterium;
  • dihydrofolate reductase;
  • enzyme catalysis;
  • IR spectroscopy;
  • noncovalent interactions

Abstract

Thumbnail image of graphical abstract

State secrets: Site-specific deuteration and FTIR studies reveal that Tyr100 in dihydrofolate reductase plays an important role in catalysis, with a strong electrostatic coupling occuring between Tyr100 and the charge that develops in the hydride-transfer transition state (see picture, NADP+ purple, Tyr100 green). However, relaying correlated motions that facilitate catalysis from distal sites of the protein to the hydride donor may also be involved.