R
Ron Wever
Researcher at University of Amsterdam
Publications - 232
Citations - 12627
Ron Wever is an academic researcher from University of Amsterdam. The author has contributed to research in topics: Vanadium bromoperoxidase & Vanadium. The author has an hindex of 57, co-authored 228 publications receiving 11845 citations. Previous affiliations of Ron Wever include University of Twente & Utrecht University.
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Tetrahydrobiopterin restores endothelial function in hypercholesterolemia.
Erik S.G. Stroes,J.J.P. Kastelein,Francesco Cosentino,Willem D. Erkelens,Ron Wever,Hendrik A. Koomans,Thomas F. Lüscher,Ton J. Rabelink +7 more
TL;DR: Restoration of endothelial dysfunction by tetrahydrobiopterin suppletion in hypercholesterolemic patients is demonstrated and both the attenuated L-mono-methyl-arginine- induced vasoconstriction as well as the impaired serotonin-induced vasodilation were restored in patients during tetrahytochemical infusion.
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V2O5 Nanowires with an Intrinsic Peroxidase-Like Activity
Rute André,Filipe Natalio,Madalena Humanes,Jana Leppin,Katja Heinze,Ron Wever,Heinz-Christoph Schröder,Werner E. G. Müller,Wolfgang Tremel +8 more
TL;DR: In this paper, the V2O5 nanowires have been shown to exhibit an intrinsic catalytic activity towards classical peroxidase substrates such as 2,2-azino-bis (ABTS) and 3,3,5,5,-tetramethylbenzdine (TMB) in the presence of H2O2.
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Vanadium pentoxide nanoparticles mimic vanadium haloperoxidases and thwart biofilm formation
Filipe Natalio,Rute André,Aloysius F. Hartog,Brigitte Stoll,Klaus Peter Jochum,Ron Wever,Wolfgang Tremel +6 more
TL;DR: It is shown that vanadium pentoxide nanowires act like naturally occurring vanadium haloperoxidases to prevent marine biofouling, and have the potential to be an alternative approach to conventional anti-bioFouling agents.
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X-ray structure of a vanadium-containing enzyme : chloroperoxidase from the fungus curvularia inaequalis
Albrecht Messerschmidt,Ron Wever +1 more
TL;DR: In this article, a crystal structure (R = 20%) of an azide chloroperoxidase complex reveals the geometry of the catalytic vanadium center, resulting in a structure with azide, three nonprotein oxygens, and a histidine as ligands.
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Demonstration by EPR spectroscopy of the functional role of iron in soybean lipoxygenase-1
J.J.M.C. de Groot,Gerrit A. Veldink,Johannes F.G. Vliegenthart,J. Boldingh,Ron Wever,B.F. Van Gelder +5 more
TL;DR: It is proposed that the enzyme with iron in the ferric state is the active species in the aerobic and anaerobic reaction of soybean lipoxygenase-1.