Unsymmetrical Binding Modes of the HOPNO Inhibitor of Tyrosinase: From Model Complexes to the Enzyme (pages 3655–3664)
Dr. Constance Bochot, Dr. Elisabeth Favre, Dr. Carole Dubois, Dr. Benoit Baptiste, Prof. Luigi Bubacco, Prof. Pierre-Alain Carrupt, Gisèle Gellon, Dr. Renaud Hardré, Prof. Dominique Luneau, Dr. Yohann Moreau, Dr. Alessandra Nurisso, Dr. Marius Réglier, Prof. Guy Serratrice, Dr. Catherine Belle and Dr. Hélène Jamet
Article first published online: 29 JAN 2013 | DOI: 10.1002/chem.201202643
An uneven bridge: The binding mode of HOPNO, a tyrosinase inhibitor, was explored by combining model complexes and theoretical computations. An unsymmetrical dicopper model complex induces an unsymmetrical bridging binding mode of HOPNO. An unsymmetrical binding mode is also obtained on the enzyme (see figure) and is linked to hydrogen-bond formation with the second coordination sphere controlling the orientation of HOPNO in the binding site.