Oxidation of substrates tethered to N-donor ligands for modeling non-heme diiron enzyme active sites

Chapter 1. Modeling Carboxylate-Rich Diiron Sites of Dioxygen-Dependent Non-Heme Enzymes Carboxylate-bridged diiron centers are employed in a variety of biological systems to activate dioxygen for substrate oxidation, and small molecule models have been synthesized to mimic this chemistry outside of the natural systems. In this introductory chapter a brief overview of terphenyl-based carboxylate systems is given and progress toward achieving structural, spectroscopic, and functional models of the protein active sites is reviewed. Chapter 2. Synthesis and Reactivity of Carboxylate-Bridged Diiron(II) Complexes with Primary Alkyl Amine Ligands The synthesis and crystallographic characterization of a series of diiron(II) complexes with sterically hindered terphenyl carboxylate ligands and alkyl amine donors are presented. The compounds ... , where ... 2,6-di(p-tolyl)benzoate, and [...] (L= NH₂(CH₂)₃SMe (4); NH₂(CH₂)₃CCH (5)), where ... is 2,6-di(3,5- dimethylphenyl)benzoate, were prepared as small molecule mimics of the catalytic sites of carboxylate-bridged non-heme diiron enzymes.

Department dc:contributor.department

Massachusetts Institute of Technology. Dept. of Chemistry.

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2005

Author dc:creator

• Carson, Emily Carrig, 1978-

Advisor dc:contributor.advisor

• Stephen J. Lippard.

• Chemistry.

Statement dc:rights

• M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission.

Licence dc:rights.uri

• http://dspace.mit.edu/handle/1721.1/7582

Language dc:language.iso

eng

Handle dc:identifier.uri

http://hdl.handle.net/1721.1/33646

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/33646