1.2- Dithiolenes cofactor biosynthesis

The final topic addressed in this chapter is the biosynthesis of the dithiolene cofactor ligand and its coordination to molybdenum and tungsten in the enzymes. Nature has clearly devised a synthetic process to overcome the twin difficulties of building a reactive dithiolene unit bearing a complicated and equally reactive pterin substituent. Molecular biology has been the tool to elucidate the steps in this complex process. Although the dithiolene formation step remains mainly a subject of conjecture, definitive information about the reagent molecule that will eventually be converted to a dithiolene is known. 

In biological systems Mo is present as the Fe/Mo cofactor of the nitrogenase enzymes (2) and of the multitude of oxidoreductases (3). In the latter the common molybdopterin cofactor (4), in addition to a dithiolene functionalized pyranopterin (5) ligand (Fig. 1), contains terminal oxo ligands and in the case of xanthine oxidase both oxo and thio ligands. Some aspects of molybdenum sulfur chemistry discussed in this work may be relevant to the biosynthesis of the molybdopterin cofactor and the function of xanthine oxidase (6). 

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