{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/23776"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/23776","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Dynamics of oxygen penetration and diffusion into horse skeletal myoglobin revealed by quenching of zinc protoporphyrin IX fluorescence","abstract":"Oxygen quenching of tryptophan fluorescence in a number of globular proteins provided some of the early experimental evidence for conformational fluctuations in proteins. Gratton et al. (Biophysical J. 1984. 45:789-794) proposed a sequential two step model called the dynamic model for oxygen quenching of internally buried fluorophores in proteins. For this study, that model is utilized to analyze the dynamics associated with conformational fluctuations of oxygen entry into the protein and to obtain thermodynamic parameters associated with these fluctuations. We used zinc protoporphyrin IX reconstituted myoglobin and performed oxygen quenching experiments at different temperatures. The data was fit to the above model and k$\\sp+$ (oxygen entry rate), k$\\sp-$ (oxygen exit rate), and $\\chi$ (oxygen migration rate) in horse skeletal myoglobin were obtained at each temperature. The activation energies were calculated using the value of k$\\sp+$ and k$\\sp-$ at each temperature. The protein-to-solvent partition coefficient for oxygen, $\\alpha$, was also obtained at each temperature along with the thermodynamic variable, $\\Delta$G, associated with this partition. The parameters k$\\sp+$, k$\\sp-$, $\\chi$, and $\\alpha$ have also been determined for the quenching of zinc protoporphyrin IX in 40% sucrose to assess the effect of viscosity on these parameters. The agreement of the steady state Stern-Volmer plot, calculated using the kinetic constants derived from the time resolved measurements with the experimental data, indicates that the dynamic model accurately represents the oxygen quenching process in horse skeletal myoglobin in all the temperature and viscosity range investigated.","abstract_html":"Oxygen quenching of tryptophan fluorescence in a number of globular proteins provided some of the early experimental evidence for conformational fluctuations in proteins. Gratton et al. (Biophysical J. 1984. 45:789-794) proposed a sequential two step model called the dynamic model for oxygen quenching of internally buried fluorophores in proteins. For this study, that model is utilized to analyze the dynamics associated with conformational fluctuations of oxygen entry into the protein and to obtain thermodynamic parameters associated with these fluctuations. We used zinc protoporphyrin IX reconstituted myoglobin and performed oxygen quenching experiments at different temperatures. The data was fit to the above model and k$\\sp+$ (oxygen entry rate), k$\\sp-$ (oxygen exit rate), and $\\chi$ (oxygen migration rate) in horse skeletal myoglobin were obtained at each temperature. The activation energies were calculated using the value of k$\\sp+$ and k$\\sp-$ at each temperature. The protein-to-solvent partition coefficient for oxygen, <span class=\"etd-inline-math\">&alpha;</span>, was also obtained at each temperature along with the thermodynamic variable, $\\Delta$G, associated with this partition. The parameters k$\\sp+$, k$\\sp-$, $\\chi$, and <span class=\"etd-inline-math\">&alpha;</span> have also been determined for the quenching of zinc protoporphyrin IX in 40% sucrose to assess the effect of viscosity on these parameters. The agreement of the steady state Stern-Volmer plot, calculated using the kinetic constants derived from the time resolved measurements with the experimental data, indicates that the dynamic model accurately represents the oxygen quenching process in horse skeletal myoglobin in all the temperature and viscosity range investigated.","abstract_has_math":true,"creators":["Carrero, Jenny"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biology, Animal Physiology","degree_department":null,"school":null,"contributors":["Gratton, E."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-05-07T14:26:39Z","date_published":"2011-05-07T14:26:39Z","updated_at":"2026-07-22T22:25:22Z","subjects":["Biology, Animal Physiology","Biophysics, General"],"languages":["eng"],"rights":["Copyright 1995 Carrero, Jenny"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9624300","(UMI)AAI9624300"],"render_values":[{"text":"AAI9624300","href":null,"code":true},{"text":"(UMI)AAI9624300","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/23776","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Gratton, E."]},{"key":"dc:creator","label":"Author","values":["Carrero, Jenny"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-05-07T14:26:39Z","10000-01-01","1995"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology, Animal Physiology","Biophysics, General"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biology, Animal Physiology","Biophysics, General"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 1995 Carrero, Jenny"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9624300","(UMI)AAI9624300","http://hdl.handle.net/2142/23776"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Oxygen quenching of tryptophan fluorescence in a number of globular proteins provided some of the early experimental evidence for conformational fluctuations in proteins. Gratton et al. (Biophysical J. 1984. 45:789-794) proposed a sequential two step model called the dynamic model for oxygen quenching of internally buried fluorophores in proteins. For this study, that model is utilized to analyze the dynamics associated with conformational fluctuations of oxygen entry into the protein and to obtain thermodynamic parameters associated with these fluctuations. We used zinc protoporphyrin IX reconstituted myoglobin and performed oxygen quenching experiments at different temperatures. The data was fit to the above model and k$\\sp+$ (oxygen entry rate), k$\\sp-$ (oxygen exit rate), and $\\chi$ (oxygen migration rate) in horse skeletal myoglobin were obtained at each temperature. The activation energies were calculated using the value of k$\\sp+$ and k$\\sp-$ at each temperature. The protein-to-solvent partition coefficient for oxygen, $\\alpha$, was also obtained at each temperature along with the thermodynamic variable, $\\Delta$G, associated with this partition. The parameters k$\\sp+$, k$\\sp-$, $\\chi$, and $\\alpha$ have also been determined for the quenching of zinc protoporphyrin IX in 40% sucrose to assess the effect of viscosity on these parameters. The agreement of the steady state Stern-Volmer plot, calculated using the kinetic constants derived from the time resolved measurements with the experimental data, indicates that the dynamic model accurately represents the oxygen quenching process in horse skeletal myoglobin in all the temperature and viscosity range investigated.","Made available in DSpace on 2011-05-07T14:26:39Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9624300.pdf: 2681113 bytes, checksum: 082faa44db80bdc4fe7f6061c89d0ca0 (MD5) Previous issue date: 1995","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T15:06:46Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:32:04-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only"]},{"key":"dc:title","label":"Title","values":["Dynamics of oxygen penetration and diffusion into horse skeletal myoglobin revealed by quenching of zinc protoporphyrin IX fluorescence"]}]}],"canonical_facts":{"dc:contributor":["Gratton, E."],"dc:creator":["Carrero, Jenny"],"dc:date":["2011-05-07T14:26:39Z","10000-01-01","1995"],"dc:description":["Oxygen quenching of tryptophan fluorescence in a number of globular proteins provided some of the early experimental evidence for conformational fluctuations in proteins. Gratton et al. (Biophysical J. 1984. 45:789-794) proposed a sequential two step model called the dynamic model for oxygen quenching of internally buried fluorophores in proteins. For this study, that model is utilized to analyze the dynamics associated with conformational fluctuations of oxygen entry into the protein and to obtain thermodynamic parameters associated with these fluctuations. We used zinc protoporphyrin IX reconstituted myoglobin and performed oxygen quenching experiments at different temperatures. The data was fit to the above model and k$\\sp+$ (oxygen entry rate), k$\\sp-$ (oxygen exit rate), and $\\chi$ (oxygen migration rate) in horse skeletal myoglobin were obtained at each temperature. The activation energies were calculated using the value of k$\\sp+$ and k$\\sp-$ at each temperature. The protein-to-solvent partition coefficient for oxygen, $\\alpha$, was also obtained at each temperature along with the thermodynamic variable, $\\Delta$G, associated with this partition. The parameters k$\\sp+$, k$\\sp-$, $\\chi$, and $\\alpha$ have also been determined for the quenching of zinc protoporphyrin IX in 40% sucrose to assess the effect of viscosity on these parameters. The agreement of the steady state Stern-Volmer plot, calculated using the kinetic constants derived from the time resolved measurements with the experimental data, indicates that the dynamic model accurately represents the oxygen quenching process in horse skeletal myoglobin in all the temperature and viscosity range investigated.","Made available in DSpace on 2011-05-07T14:26:39Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9624300.pdf: 2681113 bytes, checksum: 082faa44db80bdc4fe7f6061c89d0ca0 (MD5) Previous issue date: 1995","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T15:06:46Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:32:04-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only"],"dc:identifier":["AAI9624300","(UMI)AAI9624300","http://hdl.handle.net/2142/23776"],"dc:language":["eng"],"dc:rights":["Copyright 1995 Carrero, Jenny"],"dc:subject":["Biology, Animal Physiology","Biophysics, General"],"dc:title":["Dynamics of oxygen penetration and diffusion into horse skeletal myoglobin revealed by quenching of zinc protoporphyrin IX fluorescence"],"dc:type":["text"],"thesis:degree_discipline":["Biology, Animal Physiology","Biophysics, General"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:22Z"}