Nickel Enzymes/Models
Barbara Zambelli,
Stefano Ciurli,
Barbara Zambelli
Department of Agro-Environmental Science and Technology, University of Bologna, Bologna, Italy
Search for more papers by this authorStefano Ciurli
Center for Magnetic Resonance, University of Firenze, Florence, Italy
Search for more papers by this authorBarbara Zambelli,
Stefano Ciurli,
Barbara Zambelli
Department of Agro-Environmental Science and Technology, University of Bologna, Bologna, Italy
Search for more papers by this authorStefano Ciurli
Center for Magnetic Resonance, University of Firenze, Florence, Italy
Search for more papers by this authorFirst published: 15 September 2010
Abstract
The biochemical properties of the metal ions in a series of nickel enzymes are briefly reviewed. In particular, the properties of urease, hydrogenase, acetyl-CoA synthase/carbon monoxide dehydrogenase, methyl coenzyme-M reductase, superoxide dismutase, and acireductone dioxygenase are discussed in terms of relationships between the structure of the Ni ions in the active site and the molecular mechanism of catalysis.
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