Gu Yifan, Ellis-Guardiola Ken, Srivastava Poonam, Lewis Jared C
Department of Chemistry, University of Chicago, 5735 S. Ellis Avenue, Chicago, IL 60637 (USA).
Chembiochem. 2015 Sep 7;16(13):1880-1883. doi: 10.1002/cbic.201500165. Epub 2015 Jul 14.
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 -5 make this artificial enzyme a promising platform for developing selective photocatalytic transformations.
制备了一种双环[6,1,0]壬炔取代的9-均三甲苯基-10-甲基吖啶鎓辅因子，并将其共价连接到一个脯氨酰寡肽酶支架上，该支架在其活性位点含有一个基因编码的4-叠氮基-L-苯丙氨酸残基。所得人工酶在空气中可见光照射下催化硫氧化反应。该反应通过从酶活性位点内的硫化物初始夺取电子而进行，并且蛋白质支架延长了吖啶鎓辅因子的荧光寿命。硫化物的活化模式以及吖啶鎓辅因子(5)在脯氨酰寡肽酶-ZA -5中的位置使这种人工酶成为开发选择性光催化转化的有前景的平台。
