Role of Protein Motions in Catalysis by Formate Dehydrogenase

Dimitri Antoniou, Steven D. Schwartz

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


We have analyzed the reaction catalyzed by formate dehydrogenase using transition path sampling. This system has recently received experimental attention using infrared spectroscopy and heavy-enzyme studies. Some of the experimental results point to the possible importance of protein motions that are coupled to the chemical step. We found that the residue Val123 that lies behind the nicotinamide ring occasionally comes into van der Waals contact with the acceptor and that in all reactive trajectories, the barrier-crossing event is preceded by this contact, meaning that the motion of Val123 is part of the reaction coordinate. Experimental results have been interpreted with a two-dimensional formula for the chemical rate, which cannot capture effects such as the one we describe.

Original languageEnglish (US)
Pages (from-to)9483-9489
Number of pages7
JournalJournal of Physical Chemistry B
Issue number43
StatePublished - Oct 29 2020

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry


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