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The pyranopterin dithiolene ligand is remarkable in terms of its geometric and electronic structure and is uniquely found in mononuclear molybdenum and tungsten enzymes. The pyranopterin dithiolene is found coordinated to the metal ion, deeply buried within the protein, and non-covalently attached to the protein via an extensive hydrogen bonding network that is enzyme-specific. However, the function of pyranopterin dithiolene in enzymatic catalysis has been difficult to determine. This focused account aims to provide an overview of what has been learned from the study of pyranopterin dithiolene model complexes of molybdenum and how these results relate to the enzyme systems. This work begins with a summary of what is known about the pyranopterin dithiolene ligand in the enzymes. We then introduce the development of inorganic small molecule complexes that model aspects of a coordinated pyranopterin dithiolene and discuss the results of detailed physical studies of the models by electronic absorption, resonance Raman, X-ray absorption and NMR spectroscopies, cyclic voltammetry, X-ray crystallography, and chemical reactivity. [ABSTRACT FROM AUTHOR]

This contribution describes the path of my nearly forty-year quest to understand the special ligand coordinated to molybdenum and tungsten ions in their respective enzymes. Through this quest, I aimed to discover why nature did not simply use a methyl group on the dithiolene that chelates Mo and W but instead chose a complicated pyranopterin. My journey sought answers through the synthesis of model Mo compounds that allowed systematic investigations of the interactions between molybdenum and pterin and molybdenum and pterin-dithiolene and revealed special features of the pyranopterin dithiolene chelate bound to molybdenum. [ABSTRACT FROM AUTHOR]