Add time:08/30/2019         Source:sciencedirect.com

The development of the coordination chemistry of dithiolene ligands is summarised, together with a consideration of the electronic structure of complexes of these ‘non-innocent’ ligands. This information provides a context for a consideration of the role of dithiolenes in natural systems, i.e. as the ligand that binds molybdenum (or tungsten) at the catalytic centre of an extensive series of enzymes. These enzymes catalyse the transfer of an oxygen atom to or from the substrate: e.g. the sulfite oxidases catalyse the conversion of sulfite to sulfate and the nitrate reductases catalyse the conversion of nitrate to nitrite. The nature of the catalytic centres of several of these enzymes has been determined and each involves one or two ‘molybdopterin’ (MPT) cofactors bound to a mononuclear metal centre via their dithiolene group. The biosynthesis of MPT is described and, given its nature, possible roles for this moiety in the function of the oxotransferase enzymes are discussed. The review concludes with a consideration of the coordination chemistry that has been stimulated by the present knowledge of the nature and function of the catalytic centres of these enzymes.

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