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3) Dali server: conservation mapping in 3D. Nucl. Acids Res. 38, W545-549. Holm L, Rosenström, P. 2010. 

4) DeVore et al., Key residues controlling phenacetin metabolism by human cytochrome P450 2A enzymes. Drug metabolism and disposition: the biological fate of chemicals 36: 2582-2590.

5) Hazelard, D., Nocquet, P.A., Compain, P., 2019. Catalytic C-H amination at its limits: challenges and solutions. Organic Chemistry Frontiers 4: 2500-2521. 

 6) Hyster et al., Enzyme-controlled nitrogen-atom transfer enables regiodivergent C-H amination. Journal of the American Chemical Society 136:15505-15508. 

 7) Pandey, A.V., and Fluck, C. E., 2013. NADPH P450 oxidoreductase: Structure, function, and pathology of diseases. Science Direct 138: 229-254.

 8) Podust, L. M., and Sherman, D. H., 2012. Diversity of P450 enzymes in the biosynthesis of natural products. Natural product reports 29: 1251-1266. 

 9) Prier et al., 2017. Enantioselective, intermolecular benzylic C-H amination catalysed by an engineered iron-heme enzyme. Nature chemistry 9: 629-634. 

10) Protein Data Bank, https://www.rcsb.org/structure/5UCW. 

11) Protein identification and analysis tools on the ExPASy server. Gasteiger, E. et. al. In J. M. Walker (Ed.) The proteomics protocols handbook. Totowa, New Jersey: Humana Press Inc. 2005. 

12) Reedy et al., 2008. Development of a heme protein structure-electrochemical function database. Nucleic Acids Research 36: D307-D313. 

13) Sevrioukova et al., 1999. Structure of a cytochrome P450-redox partner electron-transfer complex. Proceedings of the National Academy of Sciences of the United States of America 96: 1863-1868.