Showing papers by "Catherine Belle published in 2009"
TL;DR: A structural model for the tyrosinase inhibition by HOPNO is proposed on the basis of results isolated and fully characterized a 1:1 (2)/OPNO adduct in which the HopNO is deprotonated and chelates only one Cu-atom of the binuclear site in a bidentate mode.
Abstract: 2-Hydroxypyridine-N-oxide (HOPNO) is described as a new and efficient transition-state analog (TS-analog) inhibitor for the mushroom tyrosinase with an IC50 = 1.16 μM and a KI = 1.8 μM. Using the binuclear copper(II) complex [Cu2(BPMP)(μ−OH)](ClO4)2 (2) known as a functional model for the tyrosinase catecholase activity, we isolated and fully characterized a 1:1 (2)/OPNO adduct in which the HOPNO is deprotonated and chelates only one Cu-atom of the binuclear site in a bidentate mode. On the basis of these results, a structural model for the tyrosinase inhibition by HOPNO is proposed.
28 citations
TL;DR: The application of solution studies in bioinorganic chemistry through paramagnetic 19F NMR is briefly reviewed in this article, where the authors summarize some theoretical aspects and select applications from bio-inorganic Chemistry (enzymes and models).
17 citations
TL;DR: In this paper, the N2(SMe)2 ligand has been synthesized and structurally characterized by X-ray crystallography, showing that the two complexes interconvert during the one electron transfer.
6 citations