Catalytic nitrile hydration is very challenging and important reaction from the perspective of both academia and industry. The metalloenzyme nitrile hydratase (NHase) catalytically hydrates nitriles into corresponding amides under ambient conditions of temperature, pressure, and physiological pH. The catalytic activity is dependent on the post-translational modification of equatorial sulfurs to sulfinate (RSO2-�) and sulfenate (RSO�) moieties at the active site containing Fe(III) or Co(III). The exact role of sulfur-oxidation has remained elusive over the years. In our efforts to understand the functioning of enzyme, we recently reported a series of functional models of enzyme employing Ru(II) that vary in the sulfur oxidation level. The series of catalysts exhibit high NHase activity as compared to other mimics. Encouraged by these results, we turned our attention to quantification of reaction rates. The effect of sulfur oxidation on reaction rate and activation parameters will be presented. DFT studies have been employed to further gain insights into catalytic cycle of nitrile hydration.

Mechanistic insights into the catalytic nitrile hydration mechanism using bioinspired mimics: Implications to nitrile hydratase

248th National Meeting (2014)

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