{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/77579"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/77579","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"The Structure and Function of Chlorophyll-Proteins in Photosystem I and The Light Harvesting Complex of Photosystem Ii","abstract":"The functional units of chloroplast membranes which mediate photosynthetic electron transport from water to NADP are structurally organized into integral complexes. Two of these membrane-bound complexes, Photosystem I (PS I) and Photosystem II (PS II), consist in part of chlorophyll proteins. The chlorophyll-protein function to absorb incident light energy and to transfer absorbed energy to photochemical reaction centers where charge separation occurs. The structure and function of the chlorophyll-proteins of PS I and the light harvesting complex of PS II have been analyzed to provide information concerning the organization of pigmented proteins in photosynthetic membranes.","abstract_html":"The functional units of chloroplast membranes which mediate photosynthetic electron transport from water to NADP are structurally organized into integral complexes. Two of these membrane-bound complexes, Photosystem I (PS I) and Photosystem II (PS II), consist in part of chlorophyll proteins. The chlorophyll-protein function to absorb incident light energy and to transfer absorbed energy to photochemical reaction centers where charge separation occurs. The structure and function of the chlorophyll-proteins of PS I and the light harvesting complex of PS II have been analyzed to provide information concerning the organization of pigmented proteins in photosynthetic membranes.","abstract_has_math":false,"creators":["Mullet, John Emerson"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-05-14T15:08:34Z","date_published":"2015-05-14T15:08:34Z","updated_at":"2026-07-22T22:26:11Z","subjects":["Biology, General"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI8127654"],"render_values":[{"text":"(UMI)AAI8127654","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/77579","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Mullet, John Emerson"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-05-14T15:08:34Z","10000-01-01","1980"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["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, General"]}]},{"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/2142/77579","(UMI)AAI8127654"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The functional units of chloroplast membranes which mediate photosynthetic electron transport from water to NADP are structurally organized into integral complexes. Two of these membrane-bound complexes, Photosystem I (PS I) and Photosystem II (PS II), consist in part of chlorophyll proteins. The chlorophyll-protein function to absorb incident light energy and to transfer absorbed energy to photochemical reaction centers where charge separation occurs. The structure and function of the chlorophyll-proteins of PS I and the light harvesting complex of PS II have been analyzed to provide information concerning the organization of pigmented proteins in photosynthetic membranes.","Photosystem I complexes were isolated by a new technique which allowed purification of PS I which retained characteristics attributed to PS I in vivo. This purified preparation of PS I was found to consist of 11 polypeptides (6-68 kilodaltons), 110 chlorophyll per P(,700), and to retain long wavelength chlorophyll a which absorbs at 700-710 nm and emits fluorescence at 730-736nm at 77K. Chlorophyll-protein complexes of PS I were reconstituted in lipid vesicles and were found by freeze-fracture analysis to be structurally organized into particles 106 (')(ANGSTROM) in diameter.","The purified PS I complexes were further fractionated by detergent treatment and PS I complexes which were depleted of chlorophyll-proteins were isolated. Depletion of 40 chlorophyll per P(,700) occurred concomitant with the loss of polypeptides of 20-25 kilodaltons and long wavelength fluorescence emission. These results led to the hypothesis that PS I contained a peripheral light harvesting chlorophyll-protein complex which was characterized by the presence of long wavelength fluorescence emission and polypeptides of 20-25 kilodaltons. This hypothesis was confirmed by studies of chlorophyll proteins which are incorporated during chloroplast development, analysis of a chlorophyll b-less barley mutant and of a mutant which lacked P700 and by fractionation of PS I with anionic detergents. Direct verification of the existence of a peripheral antennae chlorophyll-protein of PS I was obtained by separation of PS I into a core complex which contains P(,700) and a chlorophyll-protein complex which lacks P(,700), but retains polypeptides of 20-25 kilodaltons and exhibits 77 K fluorescence emission at 730-736nm.","The major chlorophyll-protein of chloroplast membranes which is structurally organized into light harvesting complexes associated with PS II was isolated and characterized and its role in thylakoid adhesion tested. The chlorophyll-protein complex, termed LHC-II, was purified by detergent treatment and sucrose gradient centrifugation. The complex consisted of 3-4 polypeptides of 25-29 kilodaltons and associated chlorophyll a and b. LHC-II particles were analyzed by freeze-fracture techniques and were found to be organized into particles of 80 (')(ANGSTROM) in diameter.","The LHC-II complexes were incorporated into lipid vesicles; this preparation was used to demonstrate the involvement of LHC-II in cross-membrane adhesion between thylakoid membranes. Adhesion in LHC-II preparations was dependent on cations and sensitive to trypsin treatment. Trypsin treatment removed peptides were isolated, analyzed and sequenced. The tryptic peptides contained a site of phosphorylation and contained significant positive charge. These structural features of LHC-II formed the basis of a proposed contact mechanism for thylakoid adhesion.","Made available in DSpace on 2015-05-14T15:08:34Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 8127654.PDF: 5037941 bytes, checksum: fcf6d13bbaa106d34ae38bd7ef8cf1ce (MD5) Previous issue date: 1980","Embargo set by: Seth Robbins for item 78789 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","150 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1980."]},{"key":"dc:title","label":"Title","values":["The Structure and Function of Chlorophyll-Proteins in Photosystem I and The Light Harvesting Complex of Photosystem Ii"]}]}],"canonical_facts":{"dc:creator":["Mullet, John Emerson"],"dc:date":["2015-05-14T15:08:34Z","10000-01-01","1980"],"dc:description":["The functional units of chloroplast membranes which mediate photosynthetic electron transport from water to NADP are structurally organized into integral complexes. Two of these membrane-bound complexes, Photosystem I (PS I) and Photosystem II (PS II), consist in part of chlorophyll proteins. The chlorophyll-protein function to absorb incident light energy and to transfer absorbed energy to photochemical reaction centers where charge separation occurs. The structure and function of the chlorophyll-proteins of PS I and the light harvesting complex of PS II have been analyzed to provide information concerning the organization of pigmented proteins in photosynthetic membranes.","Photosystem I complexes were isolated by a new technique which allowed purification of PS I which retained characteristics attributed to PS I in vivo. This purified preparation of PS I was found to consist of 11 polypeptides (6-68 kilodaltons), 110 chlorophyll per P(,700), and to retain long wavelength chlorophyll a which absorbs at 700-710 nm and emits fluorescence at 730-736nm at 77K. Chlorophyll-protein complexes of PS I were reconstituted in lipid vesicles and were found by freeze-fracture analysis to be structurally organized into particles 106 (')(ANGSTROM) in diameter.","The purified PS I complexes were further fractionated by detergent treatment and PS I complexes which were depleted of chlorophyll-proteins were isolated. Depletion of 40 chlorophyll per P(,700) occurred concomitant with the loss of polypeptides of 20-25 kilodaltons and long wavelength fluorescence emission. These results led to the hypothesis that PS I contained a peripheral light harvesting chlorophyll-protein complex which was characterized by the presence of long wavelength fluorescence emission and polypeptides of 20-25 kilodaltons. This hypothesis was confirmed by studies of chlorophyll proteins which are incorporated during chloroplast development, analysis of a chlorophyll b-less barley mutant and of a mutant which lacked P700 and by fractionation of PS I with anionic detergents. Direct verification of the existence of a peripheral antennae chlorophyll-protein of PS I was obtained by separation of PS I into a core complex which contains P(,700) and a chlorophyll-protein complex which lacks P(,700), but retains polypeptides of 20-25 kilodaltons and exhibits 77 K fluorescence emission at 730-736nm.","The major chlorophyll-protein of chloroplast membranes which is structurally organized into light harvesting complexes associated with PS II was isolated and characterized and its role in thylakoid adhesion tested. The chlorophyll-protein complex, termed LHC-II, was purified by detergent treatment and sucrose gradient centrifugation. The complex consisted of 3-4 polypeptides of 25-29 kilodaltons and associated chlorophyll a and b. LHC-II particles were analyzed by freeze-fracture techniques and were found to be organized into particles of 80 (')(ANGSTROM) in diameter.","The LHC-II complexes were incorporated into lipid vesicles; this preparation was used to demonstrate the involvement of LHC-II in cross-membrane adhesion between thylakoid membranes. Adhesion in LHC-II preparations was dependent on cations and sensitive to trypsin treatment. Trypsin treatment removed peptides were isolated, analyzed and sequenced. The tryptic peptides contained a site of phosphorylation and contained significant positive charge. These structural features of LHC-II formed the basis of a proposed contact mechanism for thylakoid adhesion.","Made available in DSpace on 2015-05-14T15:08:34Z (GMT). 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