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The Caradonna research group is interested in understanding the mechanism of action of non-heme iron metalloproteins, with a focus on the chemistry of metalloenzyme active sites involved in biological oxidation reactions. Our efforts span the continuum from the investigation of small molecule synthetic complexes that catalyze oxygen atom transfer reactions, to the characterization of an interesting class of iron/pterin-dependent aromatic amino acid hydroxylases (phenylalanine, tyrosine, and tryptophan hydroxylases), to the computational design of functional metalloproteins (iron-sulfur-based electron transfer clusters, Fe and Mn superoxide dismutanse). A broad-based approach, including chemical, molecular biological, and biophysical (spectroscopic) techniques, is used to develop a global understanding of the intrinsic characteristics of the active site metal centers and the role played by the protein matrix in regulating, modulating, and tunning these properties. |
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