Surprising cofactors in metalloenzymes

Curr Opin Struct Biol. 2003 Apr;13(2):220-6. doi: 10.1016/s0959-440x(03)00038-1.

Abstract

Transition metal complexes are located at the active sites of a number of enzymes involved in intriguing biochemical reactions. These complexes can exhibit a wide variety of chemical reactivity due to the ease at which transition metals can adopt different coordination environments and oxidation states. Crystallography has been a powerful technique for examining the structure and conformational variability of complex biological metallocenters. In particular, the past ten years have provided a wealth of structural information and several surprises concerning the metallocenters at the active sites of nitrogenase, hydrogenase and carbon monoxide dehydrogenase/acetyl-coenzyme A synthase.

Publication types

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

MeSH terms

  • Aldehyde Oxidoreductases / chemistry*
  • Aldehyde Oxidoreductases / metabolism
  • Binding Sites
  • Coenzymes / chemistry
  • Coenzymes / metabolism
  • Crystallography / methods*
  • Enzyme Activation
  • Hydrogenase / chemistry*
  • Hydrogenase / metabolism
  • Iron / chemistry*
  • Metals / chemistry
  • Metals / metabolism
  • Models, Molecular*
  • Multienzyme Complexes / chemistry*
  • Multienzyme Complexes / metabolism
  • Nickel / chemistry*
  • Nitrogenase / chemistry*
  • Nitrogenase / metabolism
  • Protein Binding
  • Protein Conformation
  • Substrate Specificity
  • Transition Elements / chemistry
  • Transition Elements / metabolism

Substances

  • Coenzymes
  • Metals
  • Multienzyme Complexes
  • Transition Elements
  • Nickel
  • Iron
  • Hydrogenase
  • Nitrogenase
  • Aldehyde Oxidoreductases
  • carbon monoxide dehydrogenase