On the Enzymatic Activation of NADH

Research output: Contribution to journalArticle

Abstract

Atomic (1 Å) resolution x-ray structures of horse liver alcohol dehydrogenase in complex with NADH revealed the formation of an adduct in the active site between a metal-bound water and NADH. Furthermore, a pronounced distortion of the pyridine ring of NADH was observed. A series of quantum chemical calculations on the water-nicotinamide adduct showed that the puckering of the pyridine ring in the crystal structures can only be reproduced when the water is considered a hydroxide ion. These observations provide fundamental insight into the enzymatic activation of NADH for hydride transfer.

Details

Authors
  • Rob Meijers
  • Richard J Morris
  • Hans W Adolph
  • Angelo Merli
  • Victor S Lamzin
  • Eila Cedergren
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biological Sciences
Original languageEnglish
Pages (from-to)9316-9321
JournalJournal of Biological Chemistry
Volume276
Issue number12
Publication statusPublished - 2001
Publication categoryResearch
Peer-reviewedYes