2 publications
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Bimetallic Copper-Heme-Protein-DNA Hybrid Catalyst for Diels Alder Reaction
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Croat. Chem. Acta 2011, 84, 269-275, 10.5562/cca1828
A bimetallic heme-DNA cofactor, containing an iron and a copper center, was synthesized for the design of novel hybrid catalysts for stereoselective synthesis. The cofactor was used for the reconstitution of apo-myoglobin. Both the cofactor alone and its myoglobin adduct were used to catalyze a model Diels Alder reaction. Stereoselectivity of this conversion was analyzed by chiral HPLC. Reactions carried out in the presence of myoglobin-heme-Cu-DNA catalyst showed greater product conversion and stereoselectivity than those carried out with the heme-Cu-DNA cofactor. This observation suggested that the protein shell plays a significant role in the catalytic conversion.
Metal: CuLigand type: BipyridineHost protein: Myoglobin (Mb)Anchoring strategy: SupramolecularOptimization: ---Notes: Horse heart myoglobin
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Structure and Function in Organometallic Protein Complexes
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J. Organomet. Chem. 2014, 751, 90-110, 10.1016/j.jorganchem.2013.07.004
Bioorganometallic chemistry is a rapidly growing subfield of organometallic chemistry. One important facet is the study of organometallic•protein complexes that contain a covalent bond between the protein and an organometallic prosthetic group. Structural elucidation of these complexes is being used with increasing frequency to determine exactly where metal binding takes place and to obtain accurate structural information. This review summarizes the structures in this field, highlighting how this information has driven the frontier of this research.
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