Selective C–H bond functionalization with light-driven P450 biocatalysts |
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Institution: | San José State University, Department of Chemistry, One Washington Square, San José, CA 95192-0101, USA |
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Abstract: | The unique photochemical properties of Ru(II)-diimine photosensitizers have enabled light-induced electron transfers in hybrid P450 heme domain enzymes. Rapid quenching of the excited state by soluble molecules generates either a highly oxidative or reductive species depending on the nature of the quencher. Under flash quench oxidative conditions, the heme cofactor of the P450 BM3 enzyme is oxidized to a high-valent ferryl species. Meanwhile, a photogenerated reductive species is able to deliver the necessary electrons to P450 heme active sites and sustain photocatalytic activity in the selective hydroxylation of substrate C–H bonds. |
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Keywords: | Bioinorganic chemistry Photochemistry C–H activation Ruthenium Enzyme catalysis Protein engineering |
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