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Published November 7, 1997 | Published
Journal Article Open

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.

Additional Information

© Royal Society of Chemistry 1997. Received 10th June 1997; Paper 7/04048B. We thank group members and M.W.W. Adams, J.H. Enemark and K.V. Rajagopalan for stimulating discussions and collaborations. This work was supported by USPHS grant GM50775 and Deutsche Forschungsgemeinschaft postdoctoral fellowships (to C.K. and H.S.). Based on the presentation given at Dalton Discussion No. 2, 2nd–5th September 1997, University of East Anglia, UK.

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August 22, 2023
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