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dc.contributor.advisorStephen J. Lippard.en_US
dc.contributor.authorBlazyk, Jessica L. (Jessica Lee), 1974-en_US
dc.contributor.otherMassachusetts Institute of Technology. Dept. of Chemistry.en_US
dc.date.accessioned2005-05-19T15:42:20Z
dc.date.available2005-05-19T15:42:20Z
dc.date.copyright2003en_US
dc.date.issued2003en_US
dc.identifier.urihttp://hdl.handle.net/1721.1/17024
dc.descriptionThesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2003.en_US
dc.descriptionVita.en_US
dc.descriptionIncludes bibliographical references.en_US
dc.descriptionThis electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections.en_US
dc.description.abstractChapter 1. Introduction: Electron Transfer in Biological Systems In many biological processes, including oxidative phosphorylation and photosynthesis, electron transfer reactions play vital roles. Electrons must be transported at catalytically relevant rates and with specificity to prevent indiscriminate electron transfer that would quickly bring cells to equilibrium. To meet these requirements, biological systems employ a panoply of organic and inorganic redox centers, most of which are sequestered within proteins. In addition to protecting a cofactor from undesirable reactions, the surrounding protein environment tunes its redox properties and mediates specific contacts with other molecules. This brief overview describes the types of redox centers used in biology, the application of electron transfer theory to physiological systems, the kinetic complexity introduced by interprotein interactions, and general mechanisms for regulating biological electron transfer. Chapter 2. Expression and Site-Directed Mutagenesis of the Reductase Component of Soluble Methane Monooxygenase from Methylococcus capsulatus (Bath) ... Chapter 3. Expression and Characterization of Ferredoxin and Flavin Adenine Dinucleotide-Binding Domains of the Reductase Component of Soluble Methane Monooxygenase from Methylococcus capsulatus (Bath) ... Chapter 4. Intermolecular Electron Transfer Reactions in Soluble Methane Monooxygenase from Methylococcus capsulatus (Bath): A Role for Hysteresis in Protein Function.en_US
dc.description.abstract(cont.) Chapter 5. Domain Engineering of the Reductase Component of Soluble Methane Monooxygenase from Methylococcus capsulatus (Bath) ... Chapter 6. Expression in Escherichia coli of the Hydroxylase Component of Soluble Methane Monooxygenase from Methylococcus capsulatus (Bath)en_US
dc.description.statementofresponsibilityby Jessica L. Blazyk.en_US
dc.format.extent312 p.en_US
dc.format.extent11247629 bytes
dc.format.extent24002513 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypeapplication/pdf
dc.language.isoengen_US
dc.publisherMassachusetts Institute of Technologyen_US
dc.rightsM.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.urihttp://dspace.mit.edu/handle/1721.1/7582
dc.subjectChemistry.en_US
dc.titleElectron transfer and protein engineering studies of the soluble methane monooxygenase from Methylococcus capsulatus (Bath)en_US
dc.typeThesisen_US
dc.description.degreePh.D.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistry
dc.identifier.oclc54495461en_US


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