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Preparation, Characterization, and Oxygenase Activity of a Photocatalytic Artificial Enzyme
Author(s) -
Gu Yifan,
EllisGuardiola Ken,
Srivastava Poonam,
Lewis Jared C.
Publication year - 2015
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201500165
Subject(s) - chemistry , cofactor , active site , covalent bond , enzyme , artificial enzyme , sulfide , residue (chemistry) , biocatalysis , combinatorial chemistry , enzyme catalysis , oxygenase , stereochemistry , catalysis , photochemistry , organic chemistry , reaction mechanism
A bicyclo[6,1,0]nonyne‐substituted 9‐mesityl‐10‐methyl‐acridinium cofactor was prepared and covalently linked to a prolyl oligopeptidase scaffold containing a genetically encoded 4‐azido‐ L ‐phenylalanine residue in its active site. The resulting artificial enzyme catalyzed sulfoxidation when irradiated with visible light in the presence of air. This reaction proceeds by initial electron abstraction from the sulfide within the enzyme active site, and the protein scaffold extended the fluorescence lifetime of the acridium cofactor. The mode of sulfide activation and placement of the acridinium cofactor ( 5 ) in POP‐ZA 4 ‐ 5 make this artificial enzyme a promising platform for developing selective photocatalytic transformations.