Abstract
Carbon monoxide dehydrogenase (CODH) and acetyl coenzyme A synthase (ACS) are environmentally important enzymes that use unprecedented nickel-containing metalloclusters to perform one-carbon chemistry using organometallic intermediates. Structural and biochemical advances have revealed the protein architectures of CODH and ACS, and in recent years the atomic compositions and geometries of their active site metalloclusters have also been resolved, leading to detailed mechanistic proposals. Here, we provide an overview of the many significant studies that have illuminated the structure and function of CODH and ACS over the last few decades while also identifying some of the critical unresolved questions that still remain.
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