Bioinorganic hydrocarbon oxidation : mechanistic and kinetic studies of the soluble methane monooxygenase from Methylococcus capsulates (bath)

Chapter 1. Principles of Small Molecule Activation by Metalloproteins as Exemplified by the Soluble Methane Monooxygenase -- Chapter 2. Small Molecule Binding to the Mixed-Valent Diiron Center of Methane Monooxygenase Hydroxylase from Methylococcus capsulatus (Bath) as Revealed by ENDOR Spectroscopy -- Chapter 3. An EPR Study of the Dinuclear Iron Site in the Soluble Methane Monooxygenase Reduced by One Electron at 77 K: the Effect of Component Interactions and the Binding of Small Molecules to the Dinuclear Ferric Center -- Chapter 4. An Investigation of the Reaction of Diferrous Methane Monooxygenase Hydroxylase with Dioxygen and Substrates by Rapid Freeze- Quench and Stopped-Flow Spectroscopy -- Chapter 5. Oxidation of Radical Clock Substrate Probes by the Soluble Methane Monooxygenase System -- Chapter 6. Tritiated Chiral Alkanes as Probes for the Mechanism of Hydroxylation by the Soluble Methane Monooxygenase.

Department dc:contributor.department

Massachusetts Institute of Technology. Department of Chemistry

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

1998

Author dc:creator

• Valentine, Ann M. (Ann Margaret), 1971-

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/1721.1/50508

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/50508