{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/25543"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/25543","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Electron spin resonance study of single crystals of cytochrome P450 from Pseudomonas putida","abstract":"The magnetic properties of the ferric heme iron in single crystals of cytochrome P450 have been studied by electron spin resonance. Spectra were recorded for orthorhombic crystals (space group P222l , 114 molecules/ unit cell) of the native, substrate-free enzyme (mo),which showed a single signal of spin S=1/2, and of the camphor complex (mos), which showed a mixture of high-spin, S=5/2, and low-spin, 8=1/2, species. Complete angular scans were taken at 9.18 GHz and temperatures of 5K' (high-spin) or 15K (low-spin) to determine the orientation of the g-tensors with respect to the crystal axes. The results are expressed in terms of the Euler angles (alpha, beta, gamma) rotating the crystal axes (c,b,a) onto the g-tensor axes (x,y,z). The O best fits of (alpha, beta, gamma) were (0,-80.-100) for m , (3,-70,-103) for 8=1/2 os os m , and (O,-95.~115) for 8=5/2 m , ,where an accidental symmetry produces the sign ambiguity. The g-values of the various species were found to be (2.48,2.25, 1.91) for mO. (2.40,2.23.1.97) for 8=1/2 mOs, and (7.75,3.93,1.80) for S=5/2 mOs; these all differed slightly from the frozen solution values. The low-spin mossignals were purely from the 1.97 species as opposed to the mixture of 1.97 and 1.91 heretofore observed in solutions. The low-spin g=2.4 was assigned to g on the basis of its near coincidence with z the high-spin g=1.8 direction. which is known to be the heme normal. The linewidths measured in the single crystal studies were consistent with the crystal mosaic distortion plus g-strain model. Best fits for the linewidth simulations were obtained with the parameter values: delta-theta = 2.2Sofor crystal mosaic spread, delta-Delta = O.ISA, deltaV = O.ISA for low-spin g-strain, and delta-alpha = 0.004 for high-spin g-strain. Unresolved hyperfine broadening was assumed to be ISG in both species based on earlier heme protein studies.","abstract_html":"The magnetic properties of the ferric heme iron in single crystals of cytochrome P450 have been studied by electron spin resonance. Spectra were recorded for orthorhombic crystals (space group P222l , 114 molecules/ unit cell) of the native, substrate-free enzyme (mo),which showed a single signal of spin S=1/2, and of the camphor complex (mos), which showed a mixture of high-spin, S=5/2, and low-spin, 8=1/2, species. Complete angular scans were taken at 9.18 GHz and temperatures of 5K' (high-spin) or 15K (low-spin) to determine the orientation of the g-tensors with respect to the crystal axes. The results are expressed in terms of the Euler angles (alpha, beta, gamma) rotating the crystal axes (c,b,a) onto the g-tensor axes (x,y,z). The O best fits of (alpha, beta, gamma) were (0,-80.-100) for m , (3,-70,-103) for 8=1/2 os os m , and (O,-95.~115) for 8=5/2 m , ,where an accidental symmetry produces the sign ambiguity. The g-values of the various species were found to be (2.48,2.25, 1.91) for mO. (2.40,2.23.1.97) for 8=1/2 mOs, and (7.75,3.93,1.80) for S=5/2 mOs; these all differed slightly from the frozen solution values. The low-spin mossignals were purely from the 1.97 species as opposed to the mixture of 1.97 and 1.91 heretofore observed in solutions. The low-spin g=2.4 was assigned to g on the basis of its near coincidence with z the high-spin g=1.8 direction. which is known to be the heme normal. The linewidths measured in the single crystal studies were consistent with the crystal mosaic distortion plus g-strain model. Best fits for the linewidth simulations were obtained with the parameter values: delta-theta = 2.2Sofor crystal mosaic spread, delta-Delta = O.ISA, deltaV = O.ISA for low-spin g-strain, and delta-alpha = 0.004 for high-spin g-strain. Unresolved hyperfine broadening was assumed to be ISG in both species based on earlier heme protein studies.","abstract_has_math":false,"creators":["Devaney, Patrick William"],"institution":null,"degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Physics","degree_department":null,"school":null,"contributors":["Debrunner, Peter G."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-06-28T14:25:03Z","date_published":"2011-06-28T14:25:03Z","updated_at":"2026-07-22T22:25:24Z","subjects":["electron spin resonance","single crystals","cytochrome P450","Pseudomonas putida","ferric heme iron"],"languages":["en"],"rights":["1980 Patrick William Devaney"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["438004"],"render_values":[{"text":"438004","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/25543","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Debrunner, Peter G."]},{"key":"dc:creator","label":"Author","values":["Devaney, Patrick William"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-06-28T14:25:03Z","10000-01-01","1980"]},{"key":"dc:type","label":"Dc Type","values":["Dissertation / Thesis","text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Physics"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["electron spin resonance","single crystals","cytochrome P450","Pseudomonas putida","ferric heme iron"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["1980 Patrick William Devaney"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["438004","http://hdl.handle.net/2142/25543"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The magnetic properties of the ferric heme iron in single crystals of cytochrome P450 have been studied by electron spin resonance. Spectra were recorded for orthorhombic crystals (space group P222l , 114 molecules/ unit cell) of the native, substrate-free enzyme (mo),which showed a single signal of spin S=1/2, and of the camphor complex (mos), which showed a mixture of high-spin, S=5/2, and low-spin, 8=1/2, species. Complete angular scans were taken at 9.18 GHz and temperatures of 5K' (high-spin) or 15K (low-spin) to determine the orientation of the g-tensors with respect to the crystal axes. The results are expressed in terms of the Euler angles (alpha, beta, gamma) rotating the crystal axes (c,b,a) onto the g-tensor axes (x,y,z). The O best fits of (alpha, beta, gamma) were (0,-80.-100) for m , (3,-70,-103) for 8=1/2 os os m , and (O,-95.~115) for 8=5/2 m , ,where an accidental symmetry produces the sign ambiguity. The g-values of the various species were found to be (2.48,2.25, 1.91) for mO. (2.40,2.23.1.97) for 8=1/2 mOs, and (7.75,3.93,1.80) for S=5/2 mOs; these all differed slightly from the frozen solution values. The low-spin mossignals were purely from the 1.97 species as opposed to the mixture of 1.97 and 1.91 heretofore observed in solutions. The low-spin g=2.4 was assigned to g on the basis of its near coincidence with z the high-spin g=1.8 direction. which is known to be the heme normal. The linewidths measured in the single crystal studies were consistent with the crystal mosaic distortion plus g-strain model. Best fits for the linewidth simulations were obtained with the parameter values: delta-theta = 2.2Sofor crystal mosaic spread, delta-Delta = O.ISA, deltaV = O.ISA for low-spin g-strain, and delta-alpha = 0.004 for high-spin g-strain. Unresolved hyperfine broadening was assumed to be ISG in both species based on earlier heme protein studies.","Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-06-28T14:25:03Z No. of bitstreams: 1 1980_devaney.pdf: 3339706 bytes, checksum: a5b7cfd8f710f7f69864f42444a82677 (MD5)","Made available in DSpace on 2011-06-28T14:25:03Z (GMT). No. of bitstreams: 1 1980_devaney.pdf: 3339706 bytes, checksum: a5b7cfd8f710f7f69864f42444a82677 (MD5) Previous issue date: 1980","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-06-28T14:25:03Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:32:22-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: Thesis","Thesis","U of I Only"]},{"key":"dc:title","label":"Title","values":["Electron spin resonance study of single crystals of cytochrome P450 from Pseudomonas putida"]}]}],"canonical_facts":{"dc:contributor":["Debrunner, Peter G."],"dc:creator":["Devaney, Patrick William"],"dc:date":["2011-06-28T14:25:03Z","10000-01-01","1980"],"dc:description":["The magnetic properties of the ferric heme iron in single crystals of cytochrome P450 have been studied by electron spin resonance. Spectra were recorded for orthorhombic crystals (space group P222l , 114 molecules/ unit cell) of the native, substrate-free enzyme (mo),which showed a single signal of spin S=1/2, and of the camphor complex (mos), which showed a mixture of high-spin, S=5/2, and low-spin, 8=1/2, species. Complete angular scans were taken at 9.18 GHz and temperatures of 5K' (high-spin) or 15K (low-spin) to determine the orientation of the g-tensors with respect to the crystal axes. The results are expressed in terms of the Euler angles (alpha, beta, gamma) rotating the crystal axes (c,b,a) onto the g-tensor axes (x,y,z). The O best fits of (alpha, beta, gamma) were (0,-80.-100) for m , (3,-70,-103) for 8=1/2 os os m , and (O,-95.~115) for 8=5/2 m , ,where an accidental symmetry produces the sign ambiguity. The g-values of the various species were found to be (2.48,2.25, 1.91) for mO. (2.40,2.23.1.97) for 8=1/2 mOs, and (7.75,3.93,1.80) for S=5/2 mOs; these all differed slightly from the frozen solution values. The low-spin mossignals were purely from the 1.97 species as opposed to the mixture of 1.97 and 1.91 heretofore observed in solutions. The low-spin g=2.4 was assigned to g on the basis of its near coincidence with z the high-spin g=1.8 direction. which is known to be the heme normal. The linewidths measured in the single crystal studies were consistent with the crystal mosaic distortion plus g-strain model. Best fits for the linewidth simulations were obtained with the parameter values: delta-theta = 2.2Sofor crystal mosaic spread, delta-Delta = O.ISA, deltaV = O.ISA for low-spin g-strain, and delta-alpha = 0.004 for high-spin g-strain. Unresolved hyperfine broadening was assumed to be ISG in both species based on earlier heme protein studies.","Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-06-28T14:25:03Z No. of bitstreams: 1 1980_devaney.pdf: 3339706 bytes, checksum: a5b7cfd8f710f7f69864f42444a82677 (MD5)","Made available in DSpace on 2011-06-28T14:25:03Z (GMT). No. of bitstreams: 1 1980_devaney.pdf: 3339706 bytes, checksum: a5b7cfd8f710f7f69864f42444a82677 (MD5) Previous issue date: 1980","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-06-28T14:25:03Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:32:22-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: Thesis","Thesis","U of I Only"],"dc:identifier":["438004","http://hdl.handle.net/2142/25543"],"dc:language":["en"],"dc:rights":["1980 Patrick William Devaney"],"dc:subject":["electron spin resonance","single crystals","cytochrome P450","Pseudomonas putida","ferric heme iron"],"dc:title":["Electron spin resonance study of single crystals of cytochrome P450 from Pseudomonas putida"],"dc:type":["Dissertation / Thesis","text"],"thesis:degree_discipline":["Physics"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."]},"updated_at":"2026-07-22T22:25:24Z"}