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Artificial Dicopper Oxidase: Rational Reprogramming of Bacterial Metallo‐β‐lactamase into a Catechol Oxidase
Author(s) -
Fujieda Nobutaka,
Hasegawa Atsuhiko,
Ishihama Kenichi,
Itoh Shinobu
Publication year - 2012
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.201101014
Subject(s) - catechol , oxidase test , reprogramming , catechol oxidase , chemistry , enzyme , mutant , biochemistry , combinatorial chemistry , hydrolysis , artificial enzyme , dioxygenase , pseudomonas , metal , stereochemistry , polyphenol oxidase , bacteria , biology , organic chemistry , cell , gene , genetics , peroxidase
Teaching metalloenzymes new tricks : An artificial type III dicopper oxidase has been developed using a hydrolytic enzyme, metallo‐β‐lactamase, as a metal‐binding platform. The triple mutant D88G/S185H/P224G redesigned by computer‐assisted structural analysis showed spectroscopic features similar to those of type III copper proteins and exhibited a high catalytic activity in the oxidation of catechols under aerobic conditions.