Sulfite oxidase molybdenum-tungsten enzymes

Figure 17.2 The structure of the pterin cofactor (1) which is common to most molybdenum- and tungsten-containing enzymes and schematic active site structures for members of the xanthine oxidase (2,3), sulfite oxidase (4) and DMSO reductase (5-7) enzyme families. (From Enemark et al., 2004. Copyright (2004) American Chemical Society.)...

Figure 16. Consensus oxidized active-site structures of the xanthine oxidase (XO), sulfite oxidase (SO), and DMSO reductase (DMSOR), and aldehyde oxidoreductase (AOR) families of mononuclear molybdenum and tungsten enzymes and the structure of the common ppd cofactor (41, 42). The question mark in the AOR structure indicates uncertainty in the presence of a coordinated water molecule.

Three human redox enzymes, and a variety of bacterial enzymes, contain molybdenum chelated by two sulfur atoms in a modified pterin molybdopterin (see Figure 10.1). In sulfite oxidase, the other two chelation sites of the molybdenum are occupied by oxygen in xanthine oxidase / dehydrogenase (Section 7.3.7) and aldehyde oxidase, one site is occupied by oxygen and one by sulfur. In some bacterial enzymes, molybdopterin occurs as a guanine dinucleotide rather than free. In others, tungsten rather than molybdopterin is the chelated metal there is no evidence that any mammalian enzymes contain tungsten. 

The chapter consists of nine sections. Sections II through VII deal with the pterin-containing molybdenum enzymes. Biochemical and model studies of molybdopterin, Mo-co, and related species are described in Section II. In Section III, we briefly survey physical and spectroscopic techniques employed in the study of the enzymes, and consider their impact upon the current understanding of the coordination about the molybdenum atom in sulfite oxidase and xanthine oxidase. Model studies are described in Sections IV and V. Section IV concentrates on structural and spectroscopic models, whereas Section V considers aspects of the reactivity of model and enzyme systems. The xanthine oxidase cycle (Section VI) and facets of intramolecular electron transfer in molybdenum enzymes (Section VII) are then treated. Section VIII describes the pterin-containing tungsten enzymes and the evolving model chemistry thereof Future directions are addressed in Section IX. 

---