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Active sites of transition-metal enzymes with a focus on nickel
Authors:Ulrich Ermler  Wolfgang Grabarse  Seigo Shima  Marcel Goubeaud  Rudolf K Thauer
Institution:aMax-Planck-Institut für Biophysik, Heinrich-Hoffmann-Straße 7, 60528 Frankfurt, Germany;bMax-Planck-Institut für terrestrische Mikrobiologie and Laboratorium für Mikrobiologie der Philipps-Universität, Karl-von-Frisch-Straße, 35043 Marburg, Germany
Abstract:Since 1995, crystal structures have been determined for many transition-metal enzymes, in particular those containing the rarely used transition metals vanadium, molybdenum, tungsten, manganese, cobalt and nickel. Accordingly, our understanding of how an enzyme uses the unique properties of a specific transition metal has been substantially increased in the past few years. The different functions of nickel in catalysis are highlighted by describing the active sites of six nickel enzymes — methyl-coenzyme M reductase, urease, hydrogenase, superoxide dismutase, carbon monoxide dehydrogenase and acetyl-coenzyme A synthase.
Keywords:Abbreviations: ACS acetyl-CoA synthase  CoA coenzyme A  CoB coenzyme B  CODH carbon monoxide dehydrogenase  CoM coenzyme M  EPR spectroscopy electron paramagnetic resonance spectroscopy  MCR methyl-CoM reductase  SOD superoxide dismutase
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