Surprising cofactors in metalloenzymes.
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.
Drennan
Catherine L
CL
Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139, USA. cdrennan@mit.edu
Peters
John W
JW
D000445:Aldehyde Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D003067:Coenzymes / Q000737:chemistry / Q000378:metabolism; D003461:Crystallography / Q000379:methods*; D004789:Enzyme Activation; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism; D007501:Iron / Q000737:chemistry*; D008670:Metals / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000378:metabolism; D009532:Nickel / Q000737:chemistry*; D009591:Nitrogenase / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D013379:Substrate Specificity; D028561:Transition Elements / Q000737:chemistry / Q000378:metabolism
D003067:Coenzymes; D008670:Metals; D009097:Multienzyme Complexes; D028561:Transition Elements; D009532:Nickel; D007501:Iron; D006864:Hydrogenase; D009591:Nitrogenase; D000445:Aldehyde Oxidoreductases; C019823:carbon monoxide dehydrogenase