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Review Article

Active sites of transition-metal enzymes with a focus on nickel

MPS-Authors
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Ermler,  Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Grabarse,  Wolfgang
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Shima,  Seigo
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

Goubeaud,  Marcel
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie der Philipps-Universität, Karl-von-Frisch-Straße, 35043 Marburg, Germany;

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Thauer,  Rudolf K.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie der Philipps-Universität, Karl-von-Frisch-Straße, 35043 Marburg, Germany;

External Resource

https://doi.org/10.1016/S0959-440X(98)80095-X
(Publisher version)

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Citation

Ermler, U., Grabarse, W., Shima, S., Goubeaud, M., & Thauer, R. K. (1998). Active sites of transition-metal enzymes with a focus on nickel. Current Opinion in Structural Biology, 8(6), 749-758. doi:10.1016/S0959-440X(98)80095-X.


Cite as: https://hdl.handle.net/21.11116/0000-0009-4B66-1
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.