{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/21339"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/21339","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Investigations of the water oxidation complex in PS II","abstract":"In this thesis an attempt was made to take the water oxidizing complex apart in a controlled way and to reconstitute it to its functional form.","abstract_html":"In this thesis an attempt was made to take the water oxidizing complex apart in a controlled way and to reconstitute it to its functional form.","abstract_has_math":false,"creators":["Shim, Hyunsuk"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biophysics","degree_department":null,"school":null,"contributors":["Debrunner, Peter G."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-05-07T13:05:47Z","date_published":"2011-05-07T13:05:47Z","updated_at":"2026-07-22T22:25:17Z","subjects":["Biology, Botany","Biophysics, General","Biology, Plant Physiology"],"languages":["eng"],"rights":["Copyright 1992 Shim, Hyunsuk"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9236593","(UMI)AAI9236593"],"render_values":[{"text":"AAI9236593","href":null,"code":true},{"text":"(UMI)AAI9236593","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/21339","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":["Shim, Hyunsuk"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-05-07T13:05:47Z","10000-01-01","1992"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biophysics"]},{"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, Botany","Biophysics, General","Biology, Plant Physiology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 1992 Shim, Hyunsuk"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9236593","(UMI)AAI9236593","http://hdl.handle.net/2142/21339"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["In this thesis an attempt was made to take the water oxidizing complex apart in a controlled way and to reconstitute it to its functional form.","The mechanism of photosynthetic water oxidation has been probed by the use of the substrate analogue NH$\\sb2$OH in 1 M NaCl treated PSII membranes lacking the 17 and 23 kD extrinsic proteins. A plot of the Mn released versus (NH$\\sb2$OH) shows a sigmoidal shape. The results were interpreted in terms of a cooperativity model. The plot of Mn release versus oxygen evolving activity shows that all 4 Mn in the reaction center are essential for active oxygen evolution.","1 M CaCl$\\sb2$ treated PSII membranes, which lack all 3 extrinsic polypeptides (17, 23, and 33 kD) have low oxygen evolving activity in spite of the full complement of 4 Mn per reaction center. If the light intensity is sufficiently low, 1 M CaCl$\\sb2$ treated PSII evolve the same number of oxygen molecules per photon as 1 M NaCl treated PSII. Therefore, removal of the 33 kD polypeptide did not inactivate the Mn center and all Mn centers are intact. When the light intensity is high, there is possible alternative electron donors to P$\\sb{680}\\sp{+}$ in 1 M CaCl$\\sb2$ treated PSII (e.g., Chl). As a result, the fluorescence and the oxygen evolving activity are low. I analyzed the fluorescence data of the S$\\sb1$ $\\to$ S$\\sb2$ transition in DCMU-treated samples. The transition time of CaCl$\\sb2$ PSII is 1.4 times longer than that of NaCl PSII. This slow-down of the S$\\sb1$ $\\to$ S$\\sb2$transition rate is not the main reason for slow donor side and there are other reports that indicate the slow-down of the S$\\sb3$ $\\to$ S$\\sb0$ transition rate. It is likely that other S state transitions, including the dark reaction, are slowed down as well.","I reconstituted 37% of the oxygen evolving activity with 40% Mn concentration in the reconstituted sample. Therefore, about 40% of the centers have all 4 Mn while the other 60% of the centers have no Mn. It is very plausible that Mn rebinding also involves cooperativity. Other divalent transition metals like Fe$\\sp{2+}$ and Co$\\sp{2+}$ apparently compete for the Mn binding sites and may form mixed metal clusters.","Made available in DSpace on 2011-05-07T13:05:47Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9236593.pdf: 4140120 bytes, checksum: 3bead66d33dbbe92e90bf38287b7ef62 (MD5) Previous issue date: 1992","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:50:06Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:22:51-05:00 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":["Investigations of the water oxidation complex in PS II"]}]}],"canonical_facts":{"dc:contributor":["Debrunner, Peter G."],"dc:creator":["Shim, Hyunsuk"],"dc:date":["2011-05-07T13:05:47Z","10000-01-01","1992"],"dc:description":["In this thesis an attempt was made to take the water oxidizing complex apart in a controlled way and to reconstitute it to its functional form.","The mechanism of photosynthetic water oxidation has been probed by the use of the substrate analogue NH$\\sb2$OH in 1 M NaCl treated PSII membranes lacking the 17 and 23 kD extrinsic proteins. A plot of the Mn released versus (NH$\\sb2$OH) shows a sigmoidal shape. The results were interpreted in terms of a cooperativity model. The plot of Mn release versus oxygen evolving activity shows that all 4 Mn in the reaction center are essential for active oxygen evolution.","1 M CaCl$\\sb2$ treated PSII membranes, which lack all 3 extrinsic polypeptides (17, 23, and 33 kD) have low oxygen evolving activity in spite of the full complement of 4 Mn per reaction center. If the light intensity is sufficiently low, 1 M CaCl$\\sb2$ treated PSII evolve the same number of oxygen molecules per photon as 1 M NaCl treated PSII. Therefore, removal of the 33 kD polypeptide did not inactivate the Mn center and all Mn centers are intact. When the light intensity is high, there is possible alternative electron donors to P$\\sb{680}\\sp{+}$ in 1 M CaCl$\\sb2$ treated PSII (e.g., Chl). As a result, the fluorescence and the oxygen evolving activity are low. I analyzed the fluorescence data of the S$\\sb1$ $\\to$ S$\\sb2$ transition in DCMU-treated samples. The transition time of CaCl$\\sb2$ PSII is 1.4 times longer than that of NaCl PSII. This slow-down of the S$\\sb1$ $\\to$ S$\\sb2$transition rate is not the main reason for slow donor side and there are other reports that indicate the slow-down of the S$\\sb3$ $\\to$ S$\\sb0$ transition rate. It is likely that other S state transitions, including the dark reaction, are slowed down as well.","I reconstituted 37% of the oxygen evolving activity with 40% Mn concentration in the reconstituted sample. Therefore, about 40% of the centers have all 4 Mn while the other 60% of the centers have no Mn. It is very plausible that Mn rebinding also involves cooperativity. Other divalent transition metals like Fe$\\sp{2+}$ and Co$\\sp{2+}$ apparently compete for the Mn binding sites and may form mixed metal clusters.","Made available in DSpace on 2011-05-07T13:05:47Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9236593.pdf: 4140120 bytes, checksum: 3bead66d33dbbe92e90bf38287b7ef62 (MD5) Previous issue date: 1992","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:50:06Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:22:51-05:00 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":["AAI9236593","(UMI)AAI9236593","http://hdl.handle.net/2142/21339"],"dc:language":["eng"],"dc:rights":["Copyright 1992 Shim, Hyunsuk"],"dc:subject":["Biology, Botany","Biophysics, General","Biology, Plant Physiology"],"dc:title":["Investigations of the water oxidation complex in PS II"],"dc:type":["text"],"thesis:degree_discipline":["Biophysics"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:17Z"}