Probing kojic acid binding to tyrosinase enzyme: insights from a model complex and QM/MM calculations.
An unambiguous picture of the interaction between the inhibitor kojic acid and a model of the dicopper active site of tyrosinase is reported. The observed binding mode probed on bacterial enzyme is confirmed and further refined by QM/MM calculations.
Département de Chimie Moléculaire, équipes CIRE et CT, Université Joseph Fourier UMR-CNRS 5250, ICMG FR-2607, BP 53, 38041, Grenoble Cedex 9, France. catherine.belle@ujf-grenoble.fr.
Constance
C
Bochot
Aurélie
A
Gouron
Luigi
L
Bubacco
Anne
A
Milet
Christian
C
Philouze
Marius
M
Réglier
Guy
G
Serratrice
Hélène
H
Jamet
Catherine
C
Belle
D020134:Catalytic Domain; D056831:Coordination Complexes / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008968:Molecular Conformation; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011485:Protein Binding; D011753:Pyrones / Q000737:chemistry / Q000378:metabolism*; D011789:Quantum Theory; D013302:Streptomyces / Q000201:enzymology
D056831:Coordination Complexes; D011753:Pyrones; C011890:kojic acid; D014442:Monophenol Monooxygenase