Bioinorganic hydrocarbon oxidation : mechanistic and kinetic studies of the soluble methane monooxygenase from Methylococcus capsulates (bath)
Name
42363712-MIT.pdf
Description
Full printable version
Size
15.6 MB
Format
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Checksum (MD5)
56afdbd78460636e49ee8399d3500f35
Author(s)
Valentine, Ann M. (Ann Margaret), 1971-
Advisor(s)
Stephen J. Lippard.
Date Issued
1998
Publisher
Massachusetts Institute of Technology
Abstract
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.
Description
Thesis (Ph.D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1998.
Includes bibliographical references (p. 219-233).
Subjects
Chemistry
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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