Evolution of strategies to prepare synthetic mimics of carboxylate-bridged diiron protein active sites
Name
Do and Lippard JIB.pdf
Size
1.29 MB
Format
Adobe PDF
Checksum (MD5)
f0d2e13519e35ddf7f2bbf98410e184c
Author(s)
Do, Loi Hung
Lippard, Stephen J.
Date Issued
September 2011
Journal
Journal of Inorganic Biochemistry
Publisher
Elsevier
Citation
Do, Loi H. and Lippard, Stephen J.“Evolution of Strategies to Prepare Synthetic Mimics of Carboxylate-Bridged Diiron Protein Active Sites.” Journal of Inorganic Biochemistry 105, no. 12 (December 2011): 1774–1785. © 2011 Elsevier Inc
Version
Author's final manuscript
Abstract
We present a comprehensive review of research conducted in our laboratory in pursuit of the long-term goal of reproducing the structures and reactivity of carboxylate-bridged diiron centers used in biology to activate dioxygen for the conversion of hydrocarbons to alcohols and related products. This article describes the evolution of strategies devised to achieve these goals and illustrates the challenges in getting there. Particular emphasis is placed on controlling the geometry and coordination environment of the diiron core, preventing formation of polynuclear iron clusters, maintaining the structural integrity of model complexes during reactions with dioxygen, and tuning the ligand framework to stabilize desired oxygenated diiron species. Studies of the various model systems have improved our understanding of the electronic and physical characteristics of carboxylate-bridged diiron units and their reactivity toward molecular oxygen and organic moieties. The principles and lessons that have emerged from these investigations will guide future efforts to develop more sophisticated diiron protein model complexes.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution-NonCommercial-NoDerivs License
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1016/j.jinorgbio.2011.08.025
