Premium
Frontispiece: Experimental and Computational Evidence for the Mechanism of Intradiol Catechol Dioxygenation by Non‐Heme Iron(III) Complexes
Author(s) -
Jastrzebski Robin,
Quesne Matthew G.,
Weckhuysen Bert M.,
de Visser Sam P.,
Bruijnincx Pieter C. A.
Publication year - 2014
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201484861
Subject(s) - catechol , chemistry , heme , cleavage (geology) , bond cleavage , enzyme , photochemistry , stereochemistry , substrate (aquarium) , reaction mechanism , mechanism (biology) , combinatorial chemistry , organic chemistry , catalysis , materials science , philosophy , oceanography , epistemology , fracture (geology) , composite material , geology
Enzyme Models Intradiol catechol dioxygenases are an important class of enzymes that catalyze the key step in the microbial degradation of aromatic compounds. In their Communication on page 15686, P. C. A. Bruijnincx and co‐workers describe their experimental and computational work on the intradiol cleavage mechanism of a biomimetic, non‐heme iron(III) complex. Surprisingly, the substrate was found to partially dissociate from the complex to enable the formation of an iron(III) superoxide intermediate. The ability of the iron(III) center to change from a high‐spin to an intermediate‐spin state was found to be crucial for activity in this formally spin‐forbidden reaction.