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A crystallographic view of the molybdenum cofactor

Rees, Douglas C. and Hu, Yonglin and Kisker, Caroline and Schindelin, Hermann (1997) A crystallographic view of the molybdenum cofactor. Journal of the Chemical Society. Dalton Transactions, 1997 (21). pp. 3909-3914. ISSN 0300-9246. doi:10.1039/a704048b.

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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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Rees, Douglas C.0000-0003-4073-1185
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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Public Health ServiceGM50775
Deutsche Forschungsgemeinschaft (DFG)UNSPECIFIED
Issue or Number:21
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ID Code:12028
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Deposited On:20 Oct 2008 19:57
Last Modified:08 Nov 2021 22:25

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