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An Efficient Light-Driven P450 BM3 Biocatalyst
犠牲的還元剤はdiethyldithiocarbamate
p450にRu錯体をつけるのは、割と古い化学。(H.B.Gray他)
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Department of Chemistry, San José State University, One Washington Square, San José, California 95192-0101, United States
J. Am. Chem. Soc., 2013, 135 (39), pp 14484–14487
DOI: 10.1021/ja409337v
Publication Date (Web): September 16, 2013
Copyright © 2013 American Chemical Society
Abstract
P450s are heme thiolate enzymes that catalyze the regio- and stereoselective functionalization of unactivated C–H bonds using molecular dioxygen and two electrons delivered by the reductase. We have developed hybrid P450 BM3 heme domains containing a covalently attached Ru(II) photosensitizer in order to circumvent the dependency on the reductase and perform P450 reactions upon visible light irradiation. A highly active hybrid enzyme with improved stability and a modified Ru(II) photosensitizer is able to catalyze the light-driven hydroxylation of lauric acid with total turnover numbers of 935 and initial reaction rate of 125 mol product/(mol enzyme/min).
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