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Oxygen Binding, Activation, and Reduction to Water by Copper Proteins
Author(s) -
Solomon Edward I.,
Chen Peng,
Metz Markus,
Lee SangKyu,
Palmer Amy E.
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(20011217)40:24<4570::aid-anie4570>3.0.co;2-4
Subject(s) - hemocyanin , chemistry , hydroxylation , oxygen , copper , copper protein , active site , photochemistry , bond cleavage , tyrosinase , stereochemistry , crystallography , enzyme , catalysis , organic chemistry , genetics , antigen , biology
Copper active sites play a major role in biological and abiological dioxygen activation. Oxygen intermediates have been studied in detail for the proteins and enzymes involved in reversible O 2 binding (hemocyanin), activation (tyrosinase), and four‐electron reduction to water (multicopper oxidases). These oxygen intermediates exhibit unique spectroscopic features indicative of new geometric and electronic structures involved in oxygen activation. The spectroscopic and quantum‐mechanical study of these intermediates has defined geometric‐ and electronic‐structure/function correlations, and developed detailed reaction coordinates for the reversible binding of O 2 , hydroxylation, and H‐atom abstraction from different substrates, and the reductive cleavage of the O−O bond in the formation water.