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

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.

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 Creators:
Ermler, Ulrich1, Author           
Grabarse, Wolfgang1, Author           
Shima, Seigo2, 3, Author
Goubeaud, Marcel 2, 3, Author
Thauer, Rudolf K.2, 3, Author
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Max-Planck-Institut für terrestrische Mikrobiologie, Marburg, Germany, ou_persistent22              
3Laboratorium für Mikrobiologie der Philipps-Universität, Karl-von-Frisch-Straße, 35043 Marburg, Germany, ou_persistent22              

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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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Language(s): eng - English
 Dates: 2002-02-251998-12
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0959-440X(98)80095-X
 Degree: -

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Title: Current Opinion in Structural Biology
  Other : Curr. Opin. Struct. Biol.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 8 (6) Sequence Number: - Start / End Page: 749 - 758 Identifier: ISSN: 0959-440X
CoNE: https://pure.mpg.de/cone/journals/resource/954925578067