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Front Cover: A Chimeric Styrene Monooxygenase with Increased Efficiency in Asymmetric Biocatalytic Epoxidation (ChemBioChem 7/2018)
Author(s) -
Corrado Maria L.,
Knaus Tanja,
Mutti Francesco G.
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800119
Subject(s) - formate dehydrogenase , monooxygenase , cofactor , chemistry , front cover , biocatalysis , styrene , formate , nad+ kinase , combinatorial chemistry , enzyme , stereochemistry , biochemistry , organic chemistry , catalysis , cover (algebra) , reaction mechanism , mechanical engineering , polymer , cytochrome p450 , engineering , copolymer
The front cover picture shows a “turbo‐snail”, which represents symbolically a fusion (Fus‐SMO) of the bi‐enzymatic system of the styrene monooxygenase from Pseudomonas sp. (StyA/StyB). The epoxidation activity of purified Fus‐SMO was up to three times higher than that of the two‐component StyA/StyB (1:1, molar ratio) system, and up to 110 times higher than that of the natural fused SMO. Furthermore, Fus‐SMO and formate dehydrogenase from Candida boidinii (Cb‐FDH) were coexpressed in Escherichia coli cells to create a self‐sufficient biocatalytic system for asymmetric epoxidation ( ee >99%) on a >500 mg scale. Thus, the “rocket” represents the system for the recycling of NAD coenzyme, which is fueled by formate. The epoxidation requires only O 2 , and generates CO 2 and H 2 O as the sole by‐products. More information can be found in the full paper by F. G. Mutti et al. on page 679 in Issue 7, 2018 (DOI: 10.1002/cbic.201700653).