Hydrogenases: Active Site Puzzles and Progress

Curr Opin Chem Biol. 2004 Apr;8(2):133-40. doi: 10.1016/j.cbpa.2004.02.004.

Abstract

Recent research on the hydrogenase reactions has sought to probe beyond the information that is provided by X-ray diffraction structures. The major challenge of locating 'transient' hydrogen atoms in species that are potential catalytic intermediates is being addressed, using advanced electron paramagnetic resonance (EPR) techniques and theoretical methods. This article discusses recent progress towards a consensus on the structures of different states of the active site of hydrogenases, the mechanisms of activation and hydrogen cycling.

Publication types

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

MeSH terms

  • Binding Sites
  • Catalysis
  • Electron Spin Resonance Spectroscopy
  • Enzyme Activation
  • Hydrogen / metabolism
  • Hydrogenase / chemistry*
  • Hydrogenase / metabolism*
  • Iron-Sulfur Proteins / chemistry*
  • Iron-Sulfur Proteins / metabolism*
  • Molecular Structure
  • Oxidation-Reduction

Substances

  • Iron-Sulfur Proteins
  • Hydrogen
  • iron hydrogenase
  • nickel-iron hydrogenase
  • Hydrogenase