Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 17, Issue 48, Pages 13482-13494Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201100665
Keywords
bioinorganic chemistry; coordination modes; copper; density functional calculations; enzyme inhibitors
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Funding
- French Agence Nationale pour la Recherche [ANR-09-BLAN-0028-01/02]
- Agence Nationale de la Recherche (ANR) [ANR-09-BLAN-0028] Funding Source: Agence Nationale de la Recherche (ANR)
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We describe 2-mercaptopyridine-N-oxide (HSPNO) as a new and efficient competitive inhibitor of mushroom tyrosinase (K-IC=3.7 mu M). Binding studies of HSPNO and 2-hydroxypyridine-N-oxide (HOPNO) on dinuclear copper(II) complexes [Cu-2(BPMP)(mu-OH)](ClO4)(2) (1; HBPMP=2,6-bis[bis(2-pyridylmethyl)aminomethyl]-4-methylphenol) and [Cu-2(BPEP)(mu-OH)](ClO4)(2)) (2; HBPEP=2,6-bis{bis[2-(2-pyridyl)ethyl]aminomethyl}-4-methylphenol), known to be functional models for the tyrosinase diphenolase activity, have been performed. A combination of structural data, spectroscopic studies, and DFT calculations evidenced the adaptable binding mode (bridging versus chelating) of HOPNO in relation to the geometry and chelate size of the dicopper center. For comparison, binding studies of HSPNO and kojic acid (5-hydroxy-2-(hydroxymethyl)-4-pyrone) on dinuclear complexes were performed. A theoretical approach has been developed and validated on HOPNO adducts to compare the binding mode on the model complexes. It has been applied for HSPNO and kojic acid. Although results for HSPNO were in line with those obtained with HOPNO, thus reflecting their chemical similarity, we showed that the bridging mode was the most preferential binding mode for kojic acid on both complexes.
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