Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9763680 | Coordination Chemistry Reviews | 2005 | 14 Pages |
Abstract
The nickel enzymes CODH and ACS (carbon monoxide dehydrogenase and acetyl-CoA synthase), as found in for example Moorella thermoacetica (formerly Clostridium thermoaceticum), play an important role in carbon cycling: the enzymes convert carbon dioxide through to cell carbon. CODH and ACS are neither structurally nor functionally related to NiFe-hydrogenase, other than that all three enzymes contain assemblies of iron, nickel and sulfur at their active sites. However, the coordination chemistry of synthetic compounds that show structural or functional analogy to the enzyme active sites has been developed in parallel. Herein will be described mono-, di- and multi-nuclear metallic complexes of relevance to the metallocentres of CODH and ACS.
Related Topics
Physical Sciences and Engineering
Chemistry
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Authors
David J. Evans,