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A Structural and Functional Model for Dioxygenases with a 2‐His‐1‐carboxylate Triad
Author(s) -
Oldenburg Paul D.,
Ke ChunYen,
Tipton A. Alex,
Shteinman Albert A.,
Que Lawrence
Publication year - 2006
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/anie.200603486
Subject(s) - carboxylate , dihydroxylation , olefin fiber , triad (sociology) , chemistry , function (biology) , ligand (biochemistry) , stereochemistry , biology , organic chemistry , biochemistry , catalysis , enantioselective synthesis , evolutionary biology , psychology , psychoanalysis , receptor
An attractive model : The iron complex shown on the left models the 2‐His‐1‐carboxylate active sites of Rieske dioxygenases both in terms of structure and function. 18 O‐labeling studies of olefin dihydroxylation support the involvement of a high‐valent iron‐oxo species.