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Multielectron Redox Catalysis with Efficient Tyrosinase Activity Based on a Visible‐Light Controlled Artificial Photoenzyme
Author(s) -
Reichl Eva,
Ertl Martin,
Knör Günther
Publication year - 2020
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.202000357
Subject(s) - chemistry , tyrosinase , redox , hydrogen peroxide , photochemistry , substrate (aquarium) , electron transfer , catalysis , combinatorial chemistry , enzyme catalysis , oxidoreductase , tyrosine , aqueous solution , enzyme kinetics , active site , enzyme , organic chemistry , biochemistry , oceanography , geology
A stepwise non‐enzymatic conversion of the natural amino acid L ‐tyrosine into physiologically relevant intermediates L ‐DOPA, dopaquinone and dopachrome has been demonstrated in aqueous solution under ambient conditions. The photocatalytic redox process applied involves controlled activation of molecular oxygen forming water and hydrogen peroxide as further reaction products. Substrate conversion can be switched on and off conveniently by regulating the degree of visible‐light or sunlight exposure of an immobilized multielectron transfer sensitizer, which is very easy to apply and can be separated again from the supernatant reaction medium. Quantitative analysis of the six‐electron redox conversion of L ‐tyrosine catalyzed by the artificial oxidoreductase enzyme system reveals a remarkable degree of abiotic phenolase activity which nearly approaches the benchmark value of the native metalloenzyme tyrosinase under substrate saturation conditions.