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Results: 122
Number of items: 122
  • Wever, R., & Hemrika, W. (1999). Vanadium in enzymes. In J. O. Nriagu (Ed.), Vanadium in the environment, part I (pp. 285-305). John Wiley & Sons.
  • ten Brink, H. B., Holland, H. L., Schoemaker, H. E., van Lingen, H., & Wever, R. (1999). Probing the scope of the sulfoxidation activity of vanadium bromoperoxidase from Ascophyllum nodosum. Tetrahedron-Asymmetry, 10, 4563-4572. https://doi.org/10.1016/S0957-4166(99)00514-5
  • Hemrika, W., Renirie, R., Macedo-Ribeiro, S., Messerschmidt, A., & Wever, R. (1999). Heterologous expression of the vanadium-containing chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and site-directed mutagenesis of the active site residues His496, Lys353, Arg360 and Arg490. The Journal of Biological Chemistry, 274, 23820-23827. https://doi.org/10.1074/jbc.274.34.23820
  • Open Access
    Kooter, I. M. (1999). On the unusual heme group of myeloperoxidase. [Thesis, fully internal, Universiteit van Amsterdam].
  • Open Access
    Tuynman, A. (1999). Enantioselective oxygen-transfer reactions catalyzed by peroxidases. [Thesis, fully internal, Universiteit van Amsterdam].
  • Hemrika, W., & Wever, R. (1997). A new model for the membrane topology of glucose-6-phosphatase: the enzyme involved in Von Gierke disease. FEBS Letters, (409), 317-319.
  • Izumi, Y., Oshiro, T., & Wever, R. (1997). Bromoperoxidase from a marine red macro-alga, Corallina pilulifera. In K. Soda, D. B. Janssen, & R. Wever (Eds.), Proceedings of the colloquium 'Mechanisms of biohalogenation and dehalogenation' (pp. 69-75). Rpyal Neth. Acad. Arts Sci..
  • Kooter, I. M., Moguilevsky, N., Bollen, A., Sijtsema, N. M., Otto, C., & Wever, R. (1997). Site-directed mutagenesis of Met 243, a residue of myeloperoxidase involved in binding of the prosthetic group. The Journal of Biological Chemistry, (2), 191-197.
  • Messerschmidt, A., Prade, P., & Wever, R. (1997). Implications for the catalytic mechanism of the vanadium-containing enzyme chloroperoxidase from the fungus Curvularia inaequalis by x-ray structures of the native and peroxide form. The Journal of Biological Chemistry, (378), 309-315.
  • Messerschmidt, A., Prade, P., & Wever, R. (1997). X-ray structures of the native and peroxide form of the vanadium-containing enzyme chloroperoxidase from the fungus Curvularia inaequalis. In K. Soda, D. B. Janssen, & R. Wever (Eds.), Proceedings of the colloquium "Mechanisms of biohalogenation and dehalogenation" (pp. 77-87). Royal Nether.l. Acad. Arts Sci.
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