Carotenoids, a family of molecules that are categorized by their alternating carbon-carbon double bonds, are responsible for a variety of important processes in all forms of life. In plants, Carotenoid Cleavage Dioxygenases (CCDs) are iron-containing enzymes capable of converting carotenoids to carotenoid derivatives (apocarotenoids), which are necessary for biological functions in all forms of life. CCDs cleave the carbon-carbon double bond, which convert carotenoids into biologically-active molecules. In this work, the study of CCDs and similar structured enzymes using small molecule model compounds were synthesized to determine the relationship between structure and reactivity. CCDs containing an iron cofactor bonded through four histidine groups (imidazole) were modeled with continual structure adjustments to imitate the active site. The complexes and oxygenated intermediates have been characterized by X-ray crystallography, Mössbauer spectroscopy, electrochemistry, DFT, NMR, IR, and UV-Vis. The relationship between structure and reactivity was further probed through reactions of model complexes with relevant organic molecules. Proposed reaction mechanisms have been developed following results of product yield.

Enzyme model complexes utilizing iron and bulky imidazole groups

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ACS Fall 2022

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