Acireductone dioxygenase (ARD) is a metalloenzyme that plays a role in the ubiquitous methionine salvage pathway (MSP) across plants, animals, and bacteria. ARD catalyzes the penultimate step in the MSP and plays a role in regulation of polyamines, carbon monoxide, and the essential amino acid methionine. Because of this regulatory role, ARD has been linked to tumor formation, carcinogenesis, and hepatitis C, making it an enzyme of particular interest. Furthermore, ARD also performs dual chemistry based solely on the metal ion bound to its active site. The iron bound analogue (Fe-ARD) performs the on-pathway reaction, whereas the nickel bound analogue (Ni-ARD) performs the off-pathway reaction. Ni-ARD and its off-pathway catalytic function, specifically, is of particular interest due to the production of carbon monoxide, a known anti-apoptotic cell signaling molecule. In order to investigate why this dual chemistry occurs and to better understand the structure-function relationship of the native enzyme, small molecular models of the active site of Ni-ARD were synthesized using a pyridine based N4O chelating ligand. Reactivity studies of this metal complex with a model substrate were performed and analyzed using 1H-NMR and UV-Vis techniques. The results point towards two potentially competitive pathways of catalytic C-C cleavage of the model substrate, which are corroborated computationally. The competitive favorability of the two reactions, one oxidative and one hydrolytic, hold significant biological implications for the native enzyme.

Biomimetic oxidative and hydrolytic reactivities of model complexes of nickel acireductone dioxygenase (Ni-ARD)

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.