Controlled halogenation of chemically versatile substrates is difficult to achieve. Here we describe a unique flavin-dependent halogenase, PltM, which is capable of utilizing a wide range of halides for installation on a diverse array of phenolic compounds, including FDA-approved drugs and natural products, such as terbutaline, fenoterol, resveratrol, and catechin. Crystal structures of PltM in complex with phloroglucinol and FAD in different states yield insight into substrate recognition and the FAD recycling mechanism of this halogenase.

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Published in Nature Communications, v. 10, article no. 1255, p. 1-11.

© The Author(s) 2019

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A correction to this article is available as the additional file listed below and online at https://doi.org/10.1038/s41467-019-09731-8.

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This work was supported by a NSF CAREER Award MCB-1149427 (to S.G.-T.), a grant as part of the National Center for Advancing Translational Sciences (UL1TR000117) (to S.G.-T. and O.V.T.), and by startup funds from the College of Pharmacy at the University of Kentucky (to S.G.-T. and O.V.T.). S.M. is a recipient of a 2018 long-term visit fellowship from the Yamada Science Foundation, Japan.

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The crystal structure coordinates and structure factor amplitudes for all crystal structures were deposited in the Protein Data Bank under accession codes 6BZN, 6BZI, 6BZA, 6BZQ, 6BZT and 6BZZ, as described in Supplementary Tables 4 and 5. NMR spectra, LC-MS, and other chromatographic data are included in the raw format in Supplementary Information. Other data are available from the corresponding authors upon reasonable request.

Supplementary Information accompanies this paper at https://doi.org/10.1038/s41467- 019-09215-9.

41467_2019_9215_MOESM1_ESM.pdf (14562 kB)
Supplementary Information

41467_2019_9215_MOESM2_ESM.pdf (71 kB)
Reporting Summary

s41467-019-09731-8.pdf (232 kB)