New catalytic model systems of tyrosinase: fine tuning of the reactivity with pyrazole-based N-donor ligands.
Two new Cu(i) complexes have been synthesized and investigated as model systems of the enzyme tyrosinase. The corresponding ligands are based on a combination of an imine function with two different pyrazole groups. The reactivity of the prepared systems with respect to the conversion of monophenols to the corresponding ortho-quinones is investigated. The resulting data are compared to results obtained for other catalytic model systems of tyrosinase.
Christian-Albrechts-Universität zu Kiel, Max-Eyth-Straße 2, 24118 Kiel, Germany. ftuczek@ac.uni-kiel.de.
Jessica Nadine
JN
Hamann
Felix
F
Tuczek
D055162:Biocatalysis; D003300:Copper / Q000737:chemistry / Q000378:metabolism; D007097:Imines / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D008958:Models, Molecular; D015394:Molecular Structure; D014442:Monophenol Monooxygenase / Q000737:chemistry / Q000378:metabolism*; D009942:Organometallic Compounds / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D011720:Pyrazoles / Q000737:chemistry / Q000378:metabolism*
D007097:Imines; D008024:Ligands; D009942:Organometallic Compounds; D011720:Pyrazoles; C031280:pyrazole; D003300:Copper; D014442:Monophenol Monooxygenase