@article{b35efd5b3aba4fbbaf730a6b90f4d6ae,
title = "A concerted mechanism for berberine bridge enzyme",
abstract = "Berberine bridge enzyme catalyzes the conversion of (S)-reticuline to (S)-scoulerine by formation of a carbon-carbon bond between the N-methyl group and the phenolic ring. We elucidated the structure of berberine bridge enzyme from Eschscholzia californica and determined the kinetic rates for three active site protein variants. Here we propose a catalytic mechanism combining base-catalyzed proton abstraction with concerted carbon-carbon coupling accompanied by hydride transfer from the N-methyl group to the N5 atom of the FAD cofactor.",
author = "Andreas Winkler and Andrzej {\L}yskowski and Sabrina Riedl and Martin Puhl and Kutchan, {Toni M.} and Peter Macheroux and Karl Gruber",
note = "Funding Information: We appreciate the support of staff scientists at the synchrotron beamlines at DESY/EMBL-Hamburg during diffraction data collection and of Hansj{\"o}rg Weber (Institute of Organic Chemistry, Graz University of Technology) for recording the NMR spectra. Financial support was provided by the Austrian Science Fund (Fonds zur F{\"o}rderung der wissenschaftlichen Forschung) through the Doktoratskolleg {\textquoteleft}{\textquoteleft}Molecular enzymology{\textquoteright}{\textquoteright} W901-B05 (to K.G. and P.M.).",
year = "2008",
month = dec,
doi = "10.1038/nchembio.123",
language = "English",
volume = "4",
pages = "739--741",
journal = "Nature Chemical Biology",
issn = "1552-4450",
number = "12",
}