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Crystal Structure Analysis of a Synthetic Non‐Heme DiironO 2 Adduct: Insight into the Mechanism of Oxygen Activation
Author(s) -
Dong Yanhong,
Yan Shiping,
Young Victor G.,
Que Lawrence
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.199606181
Subject(s) - adduct , chemistry , carboxylate , methane monooxygenase , heme , crystal structure , ligand (biochemistry) , stereochemistry , active site , oxygen , oxidoreductase , ribonucleotide reductase , enzyme , crystallography , organic chemistry , biochemistry , receptor , protein subunit , gene
The enhanced stability provided by two triphenylphosphane oxide ligands has enabled the first crystal structure analysis of a non‐heme diironO 2 adduct ( 1 ) (structure of the core is shown on the right). Complexes of this type can be activated by introducing a more electron‐donating carboxylate ligand. These observations rationalize the carboxylate‐rich active sites of non‐heme diiron oxygen‐activating enzymes such as methane monooxygenase and ribonucleotide reductase. [Fe 2 (μ‐1,2,O 2 )(N‐Et‐hptb)(Ph 3 PO) 2 ](BF 4 ) 3 1
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