{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/85481"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/85481","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Electron Transfer on the Donor and Acceptor Sides of Photosystem II Explored by Site-Directed Mutagenesis and Kinetic Spectroscopy","abstract":"H252Q and six donor-side mutants became the important tools to investigate a new model of neutral tyrosine radical, $\\rm Y\\sb{Z}\\sp\\cdot,$ introduced by Gilchrist et al. (1995) and Hoganson et al. (1995). In this new model, $\\rm Y\\sb{Z}$ is not simply a redox active residue in the electron transfer reactions, but is also directly involved in the water-oxidation. The models are critically-dependent on the presence of a neutral radical form of $\\rm Y\\sb{Z}\\ (Y\\sb{Z}\\sp{\\cdot}).$ The donor-side mutants, $\\rm E189 > L,Q,$ and $\\rm N191 > A,D,L,$ had only small effects on the pH-dependence of the rate of Q$\\rm\\sb{A}\\sp-$ and oxidized $\\rm Y\\sb{Z}$ recombination. On the other hand, E189D mutant showed a pH-independent in rate of $\\rm Q\\sb{A}\\sp-$ and oxidized $\\rm Y\\sb{Z}$ recombination. Based on these data, a simple thermodynamic model was introduced to explain the results and the model of $\\rm Y\\sb{Z}\\sp{\\cdot}$ as an oxidized form.","abstract_html":"H252Q and six donor-side mutants became the important tools to investigate a new model of neutral tyrosine radical, $\\rm Y\\sb{Z}\\sp\\cdot,$ introduced by Gilchrist et al. (1995) and Hoganson et al. (1995). In this new model, $\\rm Y\\sb{Z}$ is not simply a redox active residue in the electron transfer reactions, but is also directly involved in the water-oxidation. The models are critically-dependent on the presence of a neutral radical form of <span class=\"etd-inline-math\">\\rm Y\\sb{Z} (Y\\sb{Z}\\sp{\\cdot}).</span> The donor-side mutants, $\\rm E189 &gt; L,Q,$ and $\\rm N191 &gt; A,D,L,$ had only small effects on the pH-dependence of the rate of Q$\\rm\\sb{A}\\sp-$ and oxidized $\\rm Y\\sb{Z}$ recombination. On the other hand, E189D mutant showed a pH-independent in rate of $\\rm Q\\sb{A}\\sp-$ and oxidized $\\rm Y\\sb{Z}$ recombination. Based on these data, a simple thermodynamic model was introduced to explain the results and the model of $\\rm Y\\sb{Z}\\sp{\\cdot}$ as an oxidized form.","abstract_has_math":true,"creators":["Kanazawa, Atsuko"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biophysics and Computational Biology","degree_department":null,"school":null,"contributors":["Crofts, Antony R."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:46:14Z","date_published":"2015-09-25T22:46:14Z","updated_at":"2026-07-22T22:26:25Z","subjects":["Biology, Plant Physiology"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9812648"],"render_values":[{"text":"(MiAaPQ)AAI9812648","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/85481","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Crofts, Antony R."]},{"key":"dc:creator","label":"Author","values":["Kanazawa, Atsuko"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:46:14Z","10000-01-01","1997"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biophysics and Computational Biology"]},{"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, Plant Physiology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/85481","(MiAaPQ)AAI9812648"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["H252Q and six donor-side mutants became the important tools to investigate a new model of neutral tyrosine radical, $\\rm Y\\sb{Z}\\sp\\cdot,$ introduced by Gilchrist et al. (1995) and Hoganson et al. (1995). In this new model, $\\rm Y\\sb{Z}$ is not simply a redox active residue in the electron transfer reactions, but is also directly involved in the water-oxidation. The models are critically-dependent on the presence of a neutral radical form of $\\rm Y\\sb{Z}\\ (Y\\sb{Z}\\sp{\\cdot}).$ The donor-side mutants, $\\rm E189 > L,Q,$ and $\\rm N191 > A,D,L,$ had only small effects on the pH-dependence of the rate of Q$\\rm\\sb{A}\\sp-$ and oxidized $\\rm Y\\sb{Z}$ recombination. On the other hand, E189D mutant showed a pH-independent in rate of $\\rm Q\\sb{A}\\sp-$ and oxidized $\\rm Y\\sb{Z}$ recombination. Based on these data, a simple thermodynamic model was introduced to explain the results and the model of $\\rm Y\\sb{Z}\\sp{\\cdot}$ as an oxidized form.","Made available in DSpace on 2015-09-25T22:46:14Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9812648.pdf: 5760899 bytes, checksum: bf5eb32f170781cab2d9be75cce2a7b8 (MD5) Previous issue date: 1997","Embargo set by: Seth Robbins for item 86762 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","174 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1997."]},{"key":"dc:title","label":"Title","values":["Electron Transfer on the Donor and Acceptor Sides of Photosystem II Explored by Site-Directed Mutagenesis and Kinetic Spectroscopy"]}]}],"canonical_facts":{"dc:contributor":["Crofts, Antony R."],"dc:creator":["Kanazawa, Atsuko"],"dc:date":["2015-09-25T22:46:14Z","10000-01-01","1997"],"dc:description":["H252Q and six donor-side mutants became the important tools to investigate a new model of neutral tyrosine radical, $\\rm Y\\sb{Z}\\sp\\cdot,$ introduced by Gilchrist et al. (1995) and Hoganson et al. (1995). In this new model, $\\rm Y\\sb{Z}$ is not simply a redox active residue in the electron transfer reactions, but is also directly involved in the water-oxidation. The models are critically-dependent on the presence of a neutral radical form of $\\rm Y\\sb{Z}\\ (Y\\sb{Z}\\sp{\\cdot}).$ The donor-side mutants, $\\rm E189 > L,Q,$ and $\\rm N191 > A,D,L,$ had only small effects on the pH-dependence of the rate of Q$\\rm\\sb{A}\\sp-$ and oxidized $\\rm Y\\sb{Z}$ recombination. On the other hand, E189D mutant showed a pH-independent in rate of $\\rm Q\\sb{A}\\sp-$ and oxidized $\\rm Y\\sb{Z}$ recombination. Based on these data, a simple thermodynamic model was introduced to explain the results and the model of $\\rm Y\\sb{Z}\\sp{\\cdot}$ as an oxidized form.","Made available in DSpace on 2015-09-25T22:46:14Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9812648.pdf: 5760899 bytes, checksum: bf5eb32f170781cab2d9be75cce2a7b8 (MD5) Previous issue date: 1997","Embargo set by: Seth Robbins for item 86762 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","174 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1997."],"dc:identifier":["http://hdl.handle.net/2142/85481","(MiAaPQ)AAI9812648"],"dc:language":["eng"],"dc:subject":["Biology, Plant Physiology"],"dc:title":["Electron Transfer on the Donor and Acceptor Sides of Photosystem II Explored by Site-Directed Mutagenesis and Kinetic Spectroscopy"],"dc:type":["text"],"thesis:degree_discipline":["Biophysics and Computational Biology"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:25Z"}