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Stephen J. Lippard. Blazyk, Jessica L. (Jessica Lee), 1974- Massachusetts Institute of Technology. Dept. of Chemistry. Massachusetts Institute of Technology. Department of Chemistry 2005-05-19T15:42:20Z 2005-05-19T15:42:20Z 2003 2003 http://hdl.handle.net/1721.1/17024 54495461 Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2003. Vita. Includes bibliographical references. This electronic version was submitted by the student author. The certified thesis is available in the Institute Archives and Special Collections. Chapter 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. (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) by Jessica L. Blazyk. Ph.D. 312 p. 11247629 bytes 24002513 bytes application/pdf application/pdf eng Massachusetts Institute of Technology 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. http://dspace.mit.edu/handle/1721.1/7582 Chemistry. Electron transfer and protein engineering studies of the soluble methane monooxygenase from Methylococcus capsulatus (Bath) Thesis application/pdf false Publication unknown unknown <Publication xmlns="https://www.openaire.eu/cerif-profile/1.1/" id="51a2fdf2-3b0c-4f2e-915f-78672a649b76"> <Type xmlns="https://www.openaire.eu/cerif-profile/vocab/COAR_Publication_Types">http://purl.org/coar/resource_type/c_1843</Type> <Language>eng</Language> <Title>Electron transfer and protein engineering studies of the soluble methane monooxygenase from Methylococcus capsulatus (Bath)</Title> <PublishedIn> <Publication> </Publication> </PublishedIn> <PublicationDate>2003</PublicationDate> <Authors> <Author> <DisplayName>Blazyk, Jessica L. (Jessica Lee), 1974-</DisplayName> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> </Authors> <Editors> </Editors> <Publishers> <Publisher> <DisplayName>Massachusetts Institute of Technology</DisplayName> <OrgUnit /> </Publisher> </Publishers> <License>http://dspace.mit.edu/handle/1721.1/7582</License> <Keyword>Chemistry.</Keyword> <Abstract>Chapter 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.</Abstract> <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)</Abstract> <Access xmlns="http://purl.org/coar/access_right" > </Access> </Publication>