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Results: 122
Number of items: 122
  • Renirie, R., Hemrika, W., & Wever, R. (2000). Peroxidase and phosphatase activity of active-site mutants of vanadium chloroperoxidase from the fungus Curvularia inaequalis. Implications for the cata;ytic mechanisms. The Journal of Biological Chemistry, 275, 11650-11657. https://doi.org/10.1074/jbc.275.16.11650
  • Almeida, M., Humanes, M., Melo, R., Silva, J. A., Da Silva, J. J., & Wever, R. (2000). Purification and characterisation of vanadium haloperoxidases from the brown alga Pelvetia canaliculata. Phytochemistry, 54, 5-11. https://doi.org/10.1016/S0031-9422(99)00602-0
  • Tuynman, A., Schoemaker, H. E., & Wever, R. (2000). Enantioselective sulfoxidations catalyzed by horseradish peroxidase, manganese peroxidase, and myeloperoxidase. Monatshefte für Chemie, 131, 687-695. https://doi.org/10.1007/s007060070097
  • Open Access
    Tuynman, A., Lutje Spelberg, J., Kooter, I. M., Schoemaker, H. E., & Wever, R. (2000). Enantioselective Epoxidation and Carbon–Carbon Bond Cleavage Catalyzed by Coprinus cinereus Peroxidase and Myeloperoxidase. The Journal of Biological Chemistry, 275(5), 3025-3030. https://doi.org/10.1074/jbc.275.5.3025
  • Open Access
    ten Brink, H. B. (2000). Oxidation reactions catalyzed by Vanadium peroxidases. [Thesis, fully internal, Universiteit van Amsterdam].
  • Macedo-Ribeiro, S., Hemrika, W., Renirie, R., Wever, R., & Messerschmidt, A. (1999). X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis. Journal of Biological Inorganic Chemistry, 4, 209-219. https://doi.org/10.1007/s007750050306
  • Kooter, I. M., Moguilevsky, N., Bollen, A., Sijtsema, N. M., Otto, C., Dekker, H. L., & Wever, R. (1999). Characterization of the Asp94 and Glu242 mutants in myeloperoxidase, the residues linking the heme group via ester bonds. European Journal of Biochemistry, 274, 26794-26802.
  • Kooter, I. M., Moguilevsky, N., Bollen, A., van der Veen, L. A., Otto, C., Dekker, H. L., & Wever, R. (1999). The sulfonium ion link in myeloperoxidase. The Journal of Biological Chemistry, 274, 26794-26802. https://doi.org/10.1074/jbc.274.38.26794
  • Kooter, I. M., Koehler, B. P., Moguilevsky, N., Bollen, A., Wever, R., & Johnson, M. K. (1999). The Met243 sulfonium ion linkage is responsible for the anomalous magnetic circular dichroism and optical spectral properties of myeloperoxidase. Journal of Biological Inorganic Chemistry, 4(6), 684-691. https://doi.org/10.1007/s007750050340
  • Kapteijn, F., Moulijn, J. A., Santen, R. A., & Wever, R. (1999). Chemical kinetics of catalyzed reactions. In P. W. N. M. van Leeuwen, R. A. van Santen, J. A. Moulijn, & B. A. Averill (Eds.), Catalysis: An integrated approach, 2nd rev. (pp. 81-106). Elsevier Press.
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