Molybdoenzymes active site structures

Stiefel, E.I. The Structure and Spectra of Molybdoenzymes Active Sites and their Models. In Molybdenum and Molybdenum Enzymes (ed. Coughlan, M.), Oxford, Pergamon Press 1980, pp. 43-98... 

A wide range of soluble redox enzymes contain one or more intrinsic [2Fe-2S]2+ +, [3Fe-4S]+ , or [4Fe S]2+ + clusters that function in electron transport chains to transfer electrons to or from nonheme Fe, Moco/Wco, corrinoid, flavin, thiamine pyrophosphate (TPP), Fe S cluster containing, or NiFe active sites. Many have been structurally and spectroscopically characterized and only a few of the most recent examples of each type are summarized here. Dioxygenases that function in the dihydroxylation of aromatics such as benzene, toluene, benzoate, naphthalene, and phthalate contain a Rieske-type [2Fe-2S] + + cluster that serves as the immediate electron donor to the monomeric nonheme Fe active site see Iron Proteins with Mononuclear Active Sites). The xanthine oxidase family of molybdoenzymes see Molybdenum MPT-containing Enzymes) contain two [2Fe-2S] + + clusters that mediate electron transfer between the Moco active site and the Other soluble molybdoen-... 

JM Berg, RH Hohn. A model for the active sites of oxo-transfer molybdoenzymes synthesis, structure and properties. J Am Chem Soc 107 917-925, 1985. 

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