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  • (-) Journals = ChemBioChem
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Discovery, biocatalytic exploration and structural analysis of a 4-ethylphenol oxidase from <em>Gulosibacter chungangensis</em>
Alvigini, L., Gran-Scheuch, A., Guo, Y., Trajkovic, M., Saifuddin, M., Fraaije, M. W., & Mattevi, A. (2021). Discovery, biocatalytic exploration and structural analysis of a 4-ethylphenol oxidase from Gulosibacter chungangensis. ChemBioChem, 22(22), 3225-3233. https://doi.org/10.1002/cbic.202100457
CYP154C5 regioselectivity in steroid hydroxylation explored by substrate modifications and protein engineering
Bracco, P., Wijma, H. J., Nicolai, B., Rodriguez Buitrago, J. A., Klünemann, T., Vila, A., … Schallmey, A. (2021). CYP154C5 regioselectivity in steroid hydroxylation explored by substrate modifications and protein engineering. ChemBioChem, 22(6), 1099-1110. https://doi.org/10.1002/cbic.202000735
Biocatalytic properties and structural analysis of eugenol oxidase from <em>Rhodococcus jostii</em> RHA1: a versatile oxidative biocatalyst
Nguyen, Q. T., de Gonzalo, G., Binda, C., Rioz-Martínez, A., Mattevi, A., & Fraaije, M. W. (2016). Biocatalytic properties and structural analysis of eugenol oxidase from Rhodococcus jostii RHA1: a versatile oxidative biocatalyst. ChemBioChem, 17(14), 1359-1366. https://doi.org/10.1002/cbic.201600148
Cytochrome P450 OxyB<sub>tei</sub> catalyzes the first phenolic coupling step in teicoplanin biosynthesis
Haslinger, K., Maximowitsch, E., Brieke, C., Koch, A., & Cryle, M. J. (2014). Cytochrome P450 OxyBtei catalyzes the first phenolic coupling step in teicoplanin biosynthesis. ChemBioChem, 15(18), 2719-2728. https://doi.org/10.1002/cbic.201402441
The structure of glycerol trinitrate reductase NerA from <em>Agrobacterium radiobacter</em> reveals the molecular reason for nitro- and ene-reductase activity in OYE homologues
Oberdorfer, G., Binter, A., Wallner, S., Durchschein, K., Hall, M., Faber, K., … Gruber, K. (2013). The structure of glycerol trinitrate reductase NerA from Agrobacterium radiobacter reveals the molecular reason for nitro- and ene-reductase activity in OYE homologues. ChemBioChem, 14(7), 836-845. https://doi.org/10.1002/cbic.201300136