Active sites of transition-metal enzymes with a focus on nickel |
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Authors: | Ulrich Ermler Wolfgang Grabarse Seigo Shima Marcel Goubeaud Rudolf K Thauer |
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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 |
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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. |
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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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