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A tethered niacin-derived pincer complex with a nickel-carbon bond in lactate racemase

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Science  03 Jul 2015:
Vol. 349, Issue 6243, pp. 66-69
DOI: 10.1126/science.aab2272

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Nickel pincers as enzyme cofactors

Organometallic nickel complexes long synthesized in the laboratory exist naturally in enzymes as well. Desguin et al. determined the structure and metal-binding residues of the Ni-containing active site in bacterial lactate racemase (see the Perspective by Zamble). A dithiodinicotinic acid mononucleotide derivative cofactor binds Ni through sulfur and carbon bonds, resembling synthetic nickel pincer complexes. Genes encoding accessory proteins involved in the synthesis of this cofactor are widely distributed in other bacteria, suggesting its involvement in other enzymes.

Science, this issue p. 66; see also p. 35

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