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Chemically Modified Amino Acids in Copper Proteins That Bind or Activate Dioxygen
Author(s) -
Halcrow Malcolm A.
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20010119)40:2<346::aid-anie346>3.0.co;2-r
Subject(s) - biogenesis , chemistry , amino acid , copper , copper protein , in vitro , aqueous solution , biochemistry , oxidase test , stereochemistry , mechanism (biology) , combinatorial chemistry , enzyme , organic chemistry , gene , philosophy , epistemology
Changing mechanisms: More than half of the known classes of copper oxidase contain a chemically modified amino acid within their active site. Recent experiments by Klinman et al. on the biogenesis of one of these, topaquinone (TPQ; see scheme), have shown that this occurs by a different mechanism from that observed for the aqueous aerobic synthesis of hydroxybenzoquinones in vitro.