Journal
NATURE CHEMISTRY
Volume 9, Issue 7, Pages 629-634Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEM.2783
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Funding
- National Science Foundation, Division of Molecular and Cellular Biosciences [MCB-1513007]
- American Recovery and Reinvestment Act (ARRA) through the National Institutes of Health Shared Instrumentation Grant Program [S10RR027203]
- Resnick Sustainability Institute
- National Science Foundation [DGE-1144469]
- Donna and Benjamin M. Rosen Bioengineering Center
- Ruth Kirschstein NIH Postdoctoral Fellowship [F32G110851]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1513007] Funding Source: National Science Foundation
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C-H bonds are ubiquitous structural units of organic molecules. Although these bonds are generally considered to be chemically inert, the recent emergence of methods for C-H functionalization promises to transform the way synthetic chemistry is performed. The intermolecular amination of C-H bonds represents a particularly desirable and challenging transformation for which no efficient, highly selective, and renewable catalysts exist. Here we report the directed evolution of an iron-containing enzymatic catalyst-based on a cytochrome P450 monooxygenase-for the highly enantioselective intermolecular amination of benzylic C-H bonds. The biocatalyst is capable of up to 1,300 turnovers, exhibits excellent enantioselectivities, and provides access to valuable benzylic amines. Iron complexes are generally poor catalysts for C-H amination: in this catalyst, the enzyme's protein framework confers activity on an otherwise unreactive iron-haem cofactor.
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