Search results
Results: 26
Number of items: 26
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Hoogenkamp, M. A., Crielaard, W., ten Cate, J. M., Wever, R., Hartog, A. F., & Renirie, R. (2009). Antimicrobial activity of vanadium chloroperoxidase on planktonic Streptococcus mutans cells and Streptococcus mutans biofilms. Caries Research, 43(5), 334-338. https://doi.org/10.1159/000231569
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Renirie, R., Dewilde, A., Pierlot, C., Wever, R., Hober, D., & Aubry, J.-M. (2008). Bactericidal and virucidal activity of the alkalophilic P395D/L241V/T343A mutant of vanadium chloroperoxidase. Journal of Applied Microbiology, 105(1), 264-270. https://doi.org/10.1111/j.1365-2672.2008.03742.x
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de Macedo-Ribeiro, S., Renirie, R., Wever, R., & Messerschmidt, A. (2008). Crystal structure of a trapped phosphate intermediate in vanadium apochloroperoxidase catalyzing a dephosphorylation reaction. Biochemistry, 47(3), 929-934. https://doi.org/10.1021/bi7018628
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Pooransingh-Margolis, N., Renirie, R., Hasan, Z., Wever, R., Vega, A. J., & Polenova, T. (2006). 51V Solid-State Magic Angle Spinning NMR Spectroscopy of Vanadium Chloroperoxidase. Journal of the American Chemical Society, 128(15), 5190-5208. https://doi.org/10.1021/ja060480f
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Hasan, Z., Renirie, R., Kerkman, R., Ruijssenaars, H. J., Hartog, A. F., & Wever, R. (2006). Laboratory-evolved Vanadium Chloroperoxidase Exhibits 100-Fold Higher Halogenating Activity at Alkaline pH: Catalytic effects from first and second coordination sphere mutations. The Journal of Biological Chemistry, 281(14), 9738-9744. https://doi.org/10.1074/jbc.M512166200
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Renirie, R., Pierlot, C., Aubry, F., Hartog, A. F., Schoemaker, H. E., Alsters, P. L., & Wever, R. (2003). Vanadium chloroperoxidase as a catalyst for hydrogen peroxide disproportionation to singlet oxygen in mildly acidic aqueous environment. Advanced Synthesis & Catalysis, 345(6-7), 849-858. https://doi.org/10.1002/adsc.200303008
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Hemrika, W., Renirie, R., & Wever, R. (2000). Glucose-6-phosphatase: a member of the newly identified HPP superfamily that consists of histidine phosphatases and vanadium-containing peroxidases and consequences for membrane topology, active site and reaction mechanism. In G. Zummer (Ed.), Membrane structure in disease and drug therapy Marcel Dekker.
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Renirie, R., Hemrika, W., Piersma, S. R., & Wever, R. (2000). Cofactor and substrate binding to vanadium chloroperoxidas determined by UV-VIS spectroscopy and evidence for high affinity for pervanadate. Biochemistry, 39, 1133-1141. https://doi.org/10.1021/bi9921790
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