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Issue 21, 1997
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A crystallographic view of the molybdenum cofactor

Abstract

The molybdenum cofactor (Moco) has been found to be associated with a diverse set of redox enzymes and contains a mononuclear molybdenum or tungsten ion co-ordinated by the dithiolene sulfurs of one or two molybdopterin {a pterin [2-amino-4(1H )-pteridinone] derivative} ligands. The remaining co-ordination sites on the metal are occupied by non-protein oxygen or sulfur species and, occasionally, amino acid side chains. The molybdopterin ligand can exhibit oxidation-state-dependent changes in structure and metal co-ordination, and may also interact with other redox groups in the enzyme. These observations suggest that the molybdopterin may participate in the various electron-transfer reactions associated with the catalytic mechanism of Moco containing enzymes.

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Article information


J. Chem. Soc., Dalton Trans., 1997, 3909-3914
Article type
Paper

A crystallographic view of the molybdenum cofactor

D. C. Rees, Y. Hu, C. Kisker and H. Schindelin, J. Chem. Soc., Dalton Trans., 1997, 3909
DOI: 10.1039/A704048B

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