P450 BM3 crystal structures reveal the role of the charged surface residue Lys/Arg184 in inversion of enantioselective styrene epoxidation†
Abstract
Solved crystal structures of P450 BM3 variants in complex with
* Corresponding authors
a
Lehrstuhl für Biotechnologie, RWTH Aachen University, Worringerweg 1, 52074 Aachen, Germany
E-mail:
u.schwaneberg@biotec.rwth-aachen.de
Fax: +49 2418022387
Tel: +49 2418024170
b HASYLAB, DESY, Notkestraße 85, 22603 Hamburg, Germany
c Molzym GmbH & Co. KG, Mary-Astell-Str. 10, Bremen, Germany
d Jacobs University Bremen, 28759 Bremen, Germany
e Biocenter Klein Flottbek, University of Hamburg, Ohnhorststr. 18, 22609 Hamburg, Germany
f European Molecular Biology Laboratory – Hamburg, c/o DESY, Hamburg, Germany
Solved crystal structures of P450 BM3 variants in complex with
A. Shehzad, S. Panneerselvam, M. Linow, M. Bocola, D. Roccatano, J. Mueller-Dieckmann, M. Wilmanns and U. Schwaneberg, Chem. Commun., 2013, 49, 4694 DOI: 10.1039/C3CC39076D
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