10.1021/acs.inorgchem.7b01418.s001
Fang Wang
Fang
Wang
Sabine Becker
Sabine
Becker
Mikael A. Minier
Mikael A.
Minier
Andrei Loas
Andrei
Loas
Megan N. Jackson
Megan N.
Jackson
Stephen J. Lippard
Stephen J.
Lippard
Tuning the Diiron Core Geometry in Carboxylate-Bridged
Macrocyclic Model Complexes Affects Their Redox Properties and Supports
Oxidation Chemistry
American Chemical Society
2017
X-ray diffraction studies
methane monooxygenase hydroxylase
phenol-imine macrocyclic ligands
Diiron Core Geometry
Carboxylate-Bridged Macrocyclic Model Complexes Affects
Me
carboxylate arm controls
COOH
CH 2 units
RNR
H 3 PIMICn
diiron core geometry
presence
Fe 2
RCO
complex
carboxylate-bridged diiron proteins
2017-09-05 18:20:23
Journal contribution
https://acs.figshare.com/articles/journal_contribution/Tuning_the_Diiron_Core_Geometry_in_Carboxylate-Bridged_Macrocyclic_Model_Complexes_Affects_Their_Redox_Properties_and_Supports_Oxidation_Chemistry/5378086
We introduce a novel platform to
mimic the coordination environment of carboxylate-bridged diiron proteins
by tethering a small, dangling internal carboxylate, (CH<sub>2</sub>)<sub><i>n</i></sub>COOH, to phenol-imine macrocyclic ligands
(H<sub>3</sub>PIMICn). In the presence of an external bulky carboxylic
acid (RCO<sub>2</sub>H), the ligands react with [Fe<sub>2</sub>(Mes)<sub>4</sub>] (Mes = 2,4,6-trimethylphenyl) to afford dinuclear [Fe<sub>2</sub>(PIMICn)(RCO<sub>2</sub>)(MeCN)] (<i>n</i> = 4–6)
complexes. X-ray diffraction studies revealed structural similarities
between these complexes and the reduced diiron active sites of proteins
such as Class I ribonucleotide reductase (RNR) R2 and soluble methane
monooxygenase hydroxylase. The number of CH<sub>2</sub> units of the
internal carboxylate arm controls the diiron core geometry, affecting
in turn the anodic peak potential of the complexes. As functional
synthetic models, these complexes facilitate the oxidation of C–H
bonds in the presence of peroxides and oxo transfer from O<sub>2</sub> to an internal phosphine moiety.