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Oxygen Activation by Mononuclear Non‐Heme Iron Proteins
Author(s) -
Nivorozhkin Alexandre L.,
Girerd JeanJacques
Publication year - 1996
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199606091
Subject(s) - heme , chemistry , biochemistry , hemeprotein , metalloprotein , peripheral blood mononuclear cell , oxygen , stereochemistry , catechol , enzyme , tyrosine , organic chemistry , in vitro
Lipid dioxygenases, tyrosine hydroxylase, bleomycin, and isopenicillin N synthase are only a few of the O 2 ‐activating mononuclear non‐heme iron‐containing biomolecules. In recent years a great deal of effort has been dedicated to the elucidation of the structures and the reaction mechanisms of these systems, as well as to the synthesis of model complexes. In many cases, an iron–peroxo species is proposed as a predominant intermediate. The picture on the right shows the structure of an extradiol catechol dioxygenase recently determined by X‐ray structure analysis.