Electron transfer and protein engineering studies of the soluble methane monooxygenase from Methylococcus capsulatus (Bath)

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.

Department dc:contributor.department

Massachusetts Institute of Technology. Dept. of Chemistry.

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2003

Author dc:creator

• Blazyk, Jessica L. (Jessica Lee), 1974-

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/1721.1/17024

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/17024