期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 59, 期 32, 页码 13385-13390出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202004733
关键词
active site dynamics; copper; copper enzymes; dioxygen activation; tyrosinase
资金
- JSPS, MEXT, Japan (JSPS KAKENHI) [JP16H01025, JP18H04270]
- JST CREST [JPMJCR16P1]
The dinuclear copper enzyme, tyrosinase, activates O-2 to form a (mu-eta(2):eta(2)-peroxido)dicopper(II) species, which hydroxylates phenols to catechols. However, the exact mechanism of phenolase reaction in the catalytic site of tyrosinase is still under debate. We herein report the near atomic resolution X-ray crystal structures of the active tyrosinases with substrate l-tyrosine. At their catalytic sites, CuA moved toward l-tyrosine (CuA1 -> CuA2), whose phenol oxygen directly coordinates to CuA2, involving the movement of CuB (CuB1 -> CuB2). The crystal structures and spectroscopic analyses of the dioxygen-bound tyrosinases demonstrated that the peroxide ligand rotated, spontaneously weakening its O-O bond. Thus, the copper migration induced by the substrate-binding is accompanied by rearrangement of the bound peroxide species so as to provide one of the peroxide oxygen atoms with access to the phenol substrate's epsilon carbon atom.
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