Probing the Surface of a Laccase for Clues towards the Design of Chemo-Enzymatic Catalysts
Tipo de documentoArtículo
Fecha de publicación2017-04
Condiciones de accesoAcceso abierto
Systems featuring a multi-copper oxidase associated with transition-metal complexes can be used to perform oxidation reactions in mild conditions. Here, a strategy is presented for achieving a controlled orientation of a ruthenium–polypyridyl graft at the surface of a fungal laccase. Laccase variants are engineered with unique surface-accessible lysine residues. Distinct ruthenium–polypyridyl-modified laccases are obtained by the reductive alkylation of lysine residues precisely located relative to the T1 copper centre of the enzyme. In none of these hybrids does the presence of the graft compromise the catalytic efficiency of the enzyme on the substrate 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid). Furthermore, the efficiency of the hybrids in olefin oxidation coupled to the light-driven reduction of O2 is highly dependent on the location of the graft at the enzyme surface. Simulated RuII–CuII electron coupling values and distances fit well the observed reactivity and could be used to guide future hybrid designs.
CitaciónRobert, V. [et al.]. Probing the Surface of a Laccase for Clues towards the Design of Chemo-Enzymatic Catalysts. "ChemPlusChem", Abril 2017, vol. 82, núm. 4, p. 607-614.
Versión del editorhttp://onlinelibrary.wiley.com/doi/10.1002/cplu.201700030/abstract