{"id":{"repo_id":"mit","oai_identifier":"oai:dspace.mit.edu:1721.1/50508"},"canonical_url":"https://search.dev.ndltd.org/etd/mit/oai:dspace.mit.edu:1721.1/50508","repository":{"repo_id":"mit","name":"MIT","base_url":"https://dspace.mit.edu/oai/request"},"display":{"title":"Bioinorganic hydrocarbon oxidation : mechanistic and kinetic studies of the soluble methane monooxygenase from Methylococcus capsulates (bath)","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.","abstract_html":"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.","abstract_has_math":false,"creators":["Valentine, Ann M. (Ann Margaret), 1971-"],"institution":"Massachusetts Institute of Technology","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":"Massachusetts Institute of Technology. Department of Chemistry","school":null,"contributors":[],"advisors":["Stephen J. Lippard."],"committee_chairs":[],"committee_members":[],"year":1998,"date_issued":"1998","date_published":"1998","updated_at":"2026-07-22T22:22:14Z","subjects":["Chemistry"],"languages":["eng"],"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."],"rights_urls":["http://dspace.mit.edu/handle/1721.1/7582"],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/1721.1/50508","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Stephen J. Lippard."]},{"key":"dc:contributor.department","label":"Department","values":["Massachusetts Institute of Technology. Department of Chemistry"]},{"key":"dc:creator","label":"Author","values":["Valentine, Ann M. 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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."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["Ph.D."]},{"key":"dc:title","label":"Title","values":["Bioinorganic hydrocarbon oxidation : mechanistic and kinetic studies of the soluble methane monooxygenase from Methylococcus capsulates (bath)"]}]}],"canonical_facts":{"dc:contributor.advisor":["Stephen J. Lippard."],"dc:contributor.department":["Massachusetts Institute of Technology. Department of Chemistry"],"dc:creator":["Valentine, Ann M. (Ann Margaret), 1971-"],"dc:date.accessioned":["2010-01-07T20:47:13Z"],"dc:date.available":["2010-01-07T20:47:13Z"],"dc:date.issued":["1998"],"dc:description":["Thesis (Ph.D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1998.","Includes bibliographical references (p. 219-233)."],"dc:description.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."],"dc:description.degree":["Ph.D."],"dc:identifier.uri":["http://hdl.handle.net/1721.1/50508"],"dc:language.iso":["eng"],"dc:publisher":["Massachusetts Institute of Technology"],"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."],"dc:rights.uri":["http://dspace.mit.edu/handle/1721.1/7582"],"dc:subject":["Chemistry"],"dc:title":["Bioinorganic hydrocarbon oxidation : mechanistic and kinetic studies of the soluble methane monooxygenase from Methylococcus capsulates (bath)"],"dc:type":["Thesis"]},"updated_at":"2026-07-22T22:22:14Z"}