Ferredoxin like centers in many metalloenzymes interacts with S-adenosylmethionine to generate stable glycyl radicals. It has been proposed that the generation of stable glycyl radicals in this manner is important in many biological processes including the biosynthesis of inorganic co-factors found at the active-site of hydrogenase. Our efforts are aimed at the preparation of metallopeptide-based ferredoxin mimics which are utilized to study these processes. The metallopeptide-based mimic is based on a modified ferredoxin sequence that will bind an [4Fe-4S] cluster. The peptide sequence is designed in such a way to ensure that the [4Fe-4S] cluster will posses an open-site, that will allow for the coordination of amino-acids and other bidentate ligands. Spectroscopic characterization and reactivity studies concerning this metallopeptide will be presented.

Interaction of amino-acids with ferredoxin-like centers in a designed metallopeptid

249th National Meeting (2015)

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