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Magnetic properties of a diferrous-water complex and ligands for modeling the active site of MMOH

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dc.contributor.advisor Stephen J. Lippard. en_US
dc.contributor.author Kelly, Amy E. (Amy Elizabeth), 1980- en_US
dc.contributor.other Massachusetts Institute of Technology. Dept. of Chemistry. en_US
dc.date.accessioned 2005-09-27T17:53:08Z
dc.date.available 2005-09-27T17:53:08Z
dc.date.copyright 2004 en_US
dc.date.issued 2004 en_US
dc.identifier.uri http://hdl.handle.net/1721.1/28705
dc.description Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2004. en_US
dc.description Vita. en_US
dc.description Includes bibliographical references. en_US
dc.description.abstract Chapter 1: The Importance of Modeling Diiron Sites in Nature.There are a variety of metalloenzymes that have nearly identical carboxylate-bridged diiron active sites. An example is sMMOH, an enzyme that catalyzes the conversion of methane to methanol. A detailed description of the active site of sMMOH[red] is given and attempts at reproducing its structure in a model complex are discussed. Chapter 2: A Diiron(II) Diaqua Complex: Modeling Water in the Active Site of sMMOH[red]. There are water molecules in the first and second coordination spheres of the diiron centers in sMMOH[red]. A carboxylate-bridged diferrous complex, [Fe₂...(THF)₂], was synthesized to incorporate the presence of water in a model complex and to investigate the function(s) of these water molecules. The synthesis, structural characterization and magnetic properties of this complex are presented. Chapter 3: Ligands for Modeling the Syn Disposition of Nitrogen Atoms in the Active Site of MMOH. The active sites of a variety of carboxylate-bridged diiron metalloenzymes are very similar and feature the syn disposition of two histidine ligands with respect to the iron-iron vector. This orientation has not yet been modeled in a diiron complex with four carboxylate ligands and a stable yet flexible platform. Such geometry may be necessary to replicate the functions of these enzymes. The syntheses of ligands intended to enforce this syn disposition are described and directions for future ligand design are outlined. en_US
dc.description.statementofresponsibility by Amy E. Kelly. en_US
dc.format.extent 76 p. en_US
dc.format.extent 2590434 bytes
dc.format.extent 2598415 bytes
dc.format.mimetype application/pdf
dc.format.mimetype application/pdf
dc.language.iso en_US
dc.publisher Massachusetts Institute of Technology en_US
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. en_US
dc.rights.uri http://dspace.mit.edu/handle/1721.1/7582
dc.subject Chemistry. en_US
dc.title Magnetic properties of a diferrous-water complex and ligands for modeling the active site of MMOH en_US
dc.type Thesis en_US
dc.description.degree S.M. en_US
dc.contributor.department Massachusetts Institute of Technology. Dept. of Chemistry. en_US
dc.identifier.oclc 59133337 en_US


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