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Characterization of non-heme iron aliphatic halogenase WelO5* from Hapalosiphon welwitschii IC-52-3: Identification of a minimal protein sequence motif that confers enzymatic chlorination specificity in the biosynthesis of welwitindolelinones
Qin Zhu and Xinyu Liu
Beilstein J. Org. Chem. 2017, 13, 1168–1173.
https://doi.org/10.3762/bjoc.13.115
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Zhu, Q.; Liu, X. Beilstein J. Org. Chem. 2017, 13, 1168–1173. doi:10.3762/bjoc.13.115
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- Crowe, C.; Molyneux, S.; Sharma, S. V.; Zhang, Y.; Gkotsi, D. S.; Connaris, H.; Goss, R. J. M. Halogenases: a palette of emerging opportunities for synthetic biology–synthetic chemistry and C–H functionalisation. Chemical Society reviews 2021, 50, 9443–9481. doi:10.1039/d0cs01551b
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