Skip to Main content Skip to Navigation
Journal articles

Versatile effects of aurone structure on mushroom tyrosinase activity

Abstract : Elucidation of the binding modes of Ty inhibitors is an important step for in-depth studies on how to regulate tyrosinase activity. In this paper we highlight the extraordinarily versatile effects of the aurone structure on mushroom Ty activity. Depending on the position of the OH group on the B-ring, aurones can behave either as substrates or as hyperbolic activators. The synthesis of a hybrid aurone through combination of an aurone moiety with HOPNO (2-hydroxypyridine N-oxide), a good metal chelate, led us to a new, efficient, mixed inhibitor for mushroom tyrosinase. Another important feature pointed out by our study is the presence of more than one site for aurone compounds on mushroom tyrosinase. Because study of the binding of the hybrid aurone was difficult to perform with the enzyme, we undertook binding studies with tyrosinase functional models in order to elucidate the binding mode (chelating vs. bridging) on a dicopper(II) center. Use of EPR combined with theoretical DFT calculations allowed us to propose a preferred chelating mode for the interaction of the hybrid aurone with a dicopper(II) center.
Document type :
Journal articles
Complete list of metadata
Contributor : Hervé Vezin Connect in order to contact the contributor
Submitted on : Friday, April 13, 2012 - 10:24:23 AM
Last modification on : Friday, August 5, 2022 - 2:37:54 PM

Links full text




C. Dubois, R. Haudecoeur, M. Orio, Catherine Belle, C. Bochot, et al.. Versatile effects of aurone structure on mushroom tyrosinase activity. ChemBioChem, Wiley-VCH Verlag, 2012, 13, pp.559 - 565. ⟨10.1002/cbic.201100716⟩. ⟨hal-00687427⟩