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Results: 26
Number of items: 26
  • Wever, R., Renirie, R., & Hollmann, F. (2021). Vanadium Chloroperoxidases as Versatile Biocatalysts. In M. Sutradhar, J. A. L. da Silva, & A. J. L. Pombeiro (Eds.), Vanadium Catalysis (pp. 548-563). (Catalysis Series; No. 41). Royal Society of Chemistry. https://doi.org/10.1039/9781839160882-00548
  • Wever, R., Krenn, B. E., & Renirie, R. (2018). Marine Vanadium-Dependent Haloperoxidases, Their Isolation, Characterization, and Application. In B. S. Moore (Ed.), Marine Enzymes and Specialized Metabolism (Vol. B, pp. 141-201). (Methods in Enzymology; Vol. 605). Academic Press. https://doi.org/10.1016/bs.mie.2018.02.026
  • Open Access
    Zhang, W., Fernandez-Fueyo, E., Ni, Y., van Schie, M., Gacs, J., Renirie, R., Wever, R., Mutti, F. G., Rother, D., Alcalde, M., & Hollmann, F. (2018). Selective aerobic oxidation reactions using a combination of photocatalytic water oxidation and enzymatic oxyfunctionalizations. Nature Catalysis, 1(1), 55-62. https://doi.org/10.1038/s41929-017-0001-5
  • Dong, J. J., Fernández-Fueyo, E., Li, J., Guo, Z., Renirie, R., Wever, R., & Hollmann, F. (2017). Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis. Chemical Communications, 53(46), 6207-6210. https://doi.org/10.1039/c7cc03368k
  • Open Access
    Fernández-Fueyo, E., Younes, S. H. H., van Rootselaar, S., Aben, R. W. M., Renirie, R., Wever, R., Holtmann, D., Rutjes, F. P. J. T., & Hollmann, F. (2016). A Biocatalytic Aza-Achmatowicz Reaction. ACS Catalysis, 6(9), 5904-5907. https://doi.org/10.1021/acscatal.6b01636
  • Gupta, R., Hou, G., Renirie, R., Wever, R., & Polenova, T. (2015). 51V NMR Crystallography of Vanadium Chloroperoxidase and Its Directed Evolution P395D/L241V/T343A Mutant: Protonation Environments of the Active Site. Journal of the American Chemical Society, 137(16), 5618-5628. https://doi.org/10.1021/jacs.5b02635
  • Fernández-Fueyo, E., van Wingerden, M., Renirie, R., Wever, R., Ni, Y., Holtmann, D., & Hollmann, F. (2015). Chemoenzymatic halogenation of phenols by using the haloperoxidase from Curvularia inaequalis. ChemCatChem, 7(24), 4035-4038. https://doi.org/10.1002/cctc.201500862
  • Wever, R., & Renirie, R. (2010). Structure and function of vanadium haloperoxidases. In H. B. Dunford (Ed.), Peroxidases and catalases: biochemistry, biophysics, biotechnology, and physiology (pp. 363-386). Hoboken, NJ.
  • Renirie, R., Charnock, J. M., Garner, C. D., & Wever, R. (2010). Vanadium K-edge XAS studies on the native and peroxo-forms of vanadium chloroperoxidase from Curvularia inaequalis. Journal of inorganic biochemistry, 104(6), 657-664. https://doi.org/10.1016/j.jinorgbio.2010.02.007
  • Renirie, R., Pierlot, C., Wever, R., & Aubry, J.-M. (2009). Singlet oxygenation in microemulsion catalysed by vanadium chloroperoxidase. Journal of Molecular Catalysis B-Enzymatic, 56(4), 259-264. https://doi.org/10.1016/j.molcatb.2008.05.014
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