H₂-driven cofactor regeneration with NAD(P)⁺-reducing hydrogenases

FEBS J. 2013 Jul;280(13):3058-68. doi: 10.1111/febs.12245. Epub 2013 Apr 17.

Abstract

A large number of industrially relevant enzymes depend upon nicotinamide cofactors, which are too expensive to be added in stoichiometric amounts. Existing NAD(P)H-recycling systems suffer from low activity, or the generation of side products. H₂-driven cofactor regeneration has the advantage of 100% atom efficiency and the use of H₂ as a cheap reducing agent, in a world where sustainable energy carriers are increasingly attractive. The state of development of H₂-driven cofactor-recycling systems and examples of their integration with enzyme reactions are summarized in this article. The O₂-tolerant NAD⁺-reducing hydrogenase from Ralstonia eutropha is a particularly attractive candidate for this approach, and we therefore discuss its catalytic properties that are relevant for technical applications.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Archaeal Proteins / metabolism*
  • Bacterial Proteins / metabolism*
  • Biocatalysis
  • Bioreactors / microbiology
  • Bioreactors / parasitology
  • Cupriavidus necator / enzymology
  • Cupriavidus necator / metabolism
  • Desulfovibrio / enzymology
  • Desulfovibrio / metabolism
  • Enzyme Stability
  • Enzymes, Immobilized / metabolism
  • Hydrogen / metabolism*
  • NAD / metabolism*
  • NADP / metabolism*
  • Oxidation-Reduction
  • Oxidoreductases / metabolism*
  • Reducing Agents / metabolism*

Substances

  • Archaeal Proteins
  • Bacterial Proteins
  • Enzymes, Immobilized
  • Reducing Agents
  • NAD
  • NADP
  • Hydrogen
  • Oxidoreductases
  • NADP-reducing hydrogenase, Desulfovibrio fructosovorans
  • hydrogen dehydrogenase