Article first published online: 4 JUN 2014
DOI: 10.1002/anie.201403654
© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
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Angewandte Chemie International Edition
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- †We wish to thank the French National Research Agency (CHARMMMAT ANR-11-LABX-0039), the 7th European Community Framework Program (PIEF-GA-2013-623255), the Institut de Chimie Moléculaire et des Matériaux d’Orsay, and the Institut de Chimie des Substances Naturelles for support and fellowships.
Catalytic CH aminations with natural enzymes have not been reported thus far. However, when a cytochrome P450 enzyme is modified by switching from an iron(III) to an iron(II) center and by mutating amino acids that are critical for the catalytic activity of this monooxygenase, this modified enzyme catalyzes the intramolecular CH amination of benzenesulfonyl azides.
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