Loading…
Kinetic nature of the thermal destabilization of LHCII macroaggregates
The main light-harvesting chl a/b pigment–protein complex of photosystem II (LHCII) in isolated state forms macroaggregates with different ultrastructure and lipid content [I. Simidjiev, V. Barzda, L. Mustardy, G. Garab, Anal. Biochem. 250 (1997) 169–175]. The thermodynamic stability of highly delip...
Saved in:
| Published in: | Journal of photochemistry and photobiology. B, Biology Biology, 2005-02, Vol.78 (2), p.165-170 |
|---|---|
| Main Authors: | , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c372t-338488f75c79943bf903b891169e5ad38df952e60e0be8f9313d5da826d611a3 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c372t-338488f75c79943bf903b891169e5ad38df952e60e0be8f9313d5da826d611a3 |
| container_end_page | 170 |
| container_issue | 2 |
| container_start_page | 165 |
| container_title | Journal of photochemistry and photobiology. B, Biology |
| container_volume | 78 |
| creator | Krumova, Sashka B. Todinova, Svetla J. Busheva, Mira C. Taneva, Stefka G. |
| description | The main light-harvesting chl
a/b pigment–protein complex of photosystem II (LHCII) in isolated state forms macroaggregates with different ultrastructure and lipid content [I. Simidjiev, V. Barzda, L. Mustardy, G. Garab, Anal. Biochem. 250 (1997) 169–175]. The thermodynamic stability of highly delipidated tightly bound LHCII macroaggregates is studied by differential scanning calorimetry and fluorescence spectroscopy. The calorimetric profile of LHCII is asymmetric, the denaturation transition is taking place at around 72 °C. A shoulder, which overlaps with the main denaturation transition, appears around 58 °C. The denaturation temperature strongly depends on the scanning rate indicating the kinetic nature of the thermal destabilization of LHCII macroaggregates. The fluorescence data prove that the thermal denaturation of LHCII is an irreversible and kinetically controlled process. |
| doi_str_mv | 10.1016/j.jphotobiol.2004.11.005 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67370988</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1011134404001745</els_id><sourcerecordid>67370988</sourcerecordid><originalsourceid>FETCH-LOGICAL-c372t-338488f75c79943bf903b891169e5ad38df952e60e0be8f9313d5da826d611a3</originalsourceid><addsrcrecordid>eNqFkE1PwzAMhiMEYmPwF1BP3Fripk3TI0x8TEzisnuUNu6WqW1GkiHBryfTJu2IJcuW_PrrISQBmgEF_rjNtruNDbYxts9ySosMIKO0vCBTEBVLcy7yy5hTgBRYUUzIjfdbGq3k1TWZQMl5UdJiSl4_zIjBtMmowt5hYrskbPDgblB9otEH1Zje_Kpg7HgoL9_ni0UyqNZZtV47XKuA_pZcdar3eHeKM7J6fVnN39Pl59ti_rRMW1blIWVMFEJ0VdlWdV2wpqspa0QNwGsslWZCd3WZI6dIGxRdzYDpUiuRc80BFJuRh-PYnbNf-3ibHIxvse_ViHbvJa9YRWsholAchfFK7x12cufMoNyPBCoPCOVWnhHKA0IJICOf2Hp_2rFvBtTnxhOzKHg-CjA--m3QSd8aHFvUxmEbpLbm_y1_QT6HIA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>67370988</pqid></control><display><type>article</type><title>Kinetic nature of the thermal destabilization of LHCII macroaggregates</title><source>ScienceDirect Journals</source><creator>Krumova, Sashka B. ; Todinova, Svetla J. ; Busheva, Mira C. ; Taneva, Stefka G.</creator><creatorcontrib>Krumova, Sashka B. ; Todinova, Svetla J. ; Busheva, Mira C. ; Taneva, Stefka G.</creatorcontrib><description>The main light-harvesting chl
a/b pigment–protein complex of photosystem II (LHCII) in isolated state forms macroaggregates with different ultrastructure and lipid content [I. Simidjiev, V. Barzda, L. Mustardy, G. Garab, Anal. Biochem. 250 (1997) 169–175]. The thermodynamic stability of highly delipidated tightly bound LHCII macroaggregates is studied by differential scanning calorimetry and fluorescence spectroscopy. The calorimetric profile of LHCII is asymmetric, the denaturation transition is taking place at around 72 °C. A shoulder, which overlaps with the main denaturation transition, appears around 58 °C. The denaturation temperature strongly depends on the scanning rate indicating the kinetic nature of the thermal destabilization of LHCII macroaggregates. The fluorescence data prove that the thermal denaturation of LHCII is an irreversible and kinetically controlled process.</description><identifier>ISSN: 1011-1344</identifier><identifier>EISSN: 1873-2682</identifier><identifier>DOI: 10.1016/j.jphotobiol.2004.11.005</identifier><identifier>PMID: 15664504</identifier><language>eng</language><publisher>Switzerland: Elsevier B.V</publisher><subject>Calorimetric enthalpy ; Calorimetry, Differential Scanning ; Denaturation transition ; Differential scanning calorimetry ; Enzyme Stability ; Fluorescence emission ; Kinetics ; Light-harvesting chlorophyll a/b pigment–protein complex ; Photosystem II Protein Complex - chemistry ; Photosystem II Protein Complex - isolation & purification ; Photosystem II Protein Complex - metabolism ; Pisum sativum - enzymology ; Protein Denaturation ; Spectrometry, Fluorescence ; Spinacia oleracea - enzymology ; Temperature</subject><ispartof>Journal of photochemistry and photobiology. B, Biology, 2005-02, Vol.78 (2), p.165-170</ispartof><rights>2004 Elsevier B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c372t-338488f75c79943bf903b891169e5ad38df952e60e0be8f9313d5da826d611a3</citedby><cites>FETCH-LOGICAL-c372t-338488f75c79943bf903b891169e5ad38df952e60e0be8f9313d5da826d611a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15664504$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Krumova, Sashka B.</creatorcontrib><creatorcontrib>Todinova, Svetla J.</creatorcontrib><creatorcontrib>Busheva, Mira C.</creatorcontrib><creatorcontrib>Taneva, Stefka G.</creatorcontrib><title>Kinetic nature of the thermal destabilization of LHCII macroaggregates</title><title>Journal of photochemistry and photobiology. B, Biology</title><addtitle>J Photochem Photobiol B</addtitle><description>The main light-harvesting chl
a/b pigment–protein complex of photosystem II (LHCII) in isolated state forms macroaggregates with different ultrastructure and lipid content [I. Simidjiev, V. Barzda, L. Mustardy, G. Garab, Anal. Biochem. 250 (1997) 169–175]. The thermodynamic stability of highly delipidated tightly bound LHCII macroaggregates is studied by differential scanning calorimetry and fluorescence spectroscopy. The calorimetric profile of LHCII is asymmetric, the denaturation transition is taking place at around 72 °C. A shoulder, which overlaps with the main denaturation transition, appears around 58 °C. The denaturation temperature strongly depends on the scanning rate indicating the kinetic nature of the thermal destabilization of LHCII macroaggregates. The fluorescence data prove that the thermal denaturation of LHCII is an irreversible and kinetically controlled process.</description><subject>Calorimetric enthalpy</subject><subject>Calorimetry, Differential Scanning</subject><subject>Denaturation transition</subject><subject>Differential scanning calorimetry</subject><subject>Enzyme Stability</subject><subject>Fluorescence emission</subject><subject>Kinetics</subject><subject>Light-harvesting chlorophyll a/b pigment–protein complex</subject><subject>Photosystem II Protein Complex - chemistry</subject><subject>Photosystem II Protein Complex - isolation & purification</subject><subject>Photosystem II Protein Complex - metabolism</subject><subject>Pisum sativum - enzymology</subject><subject>Protein Denaturation</subject><subject>Spectrometry, Fluorescence</subject><subject>Spinacia oleracea - enzymology</subject><subject>Temperature</subject><issn>1011-1344</issn><issn>1873-2682</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNqFkE1PwzAMhiMEYmPwF1BP3Fripk3TI0x8TEzisnuUNu6WqW1GkiHBryfTJu2IJcuW_PrrISQBmgEF_rjNtruNDbYxts9ySosMIKO0vCBTEBVLcy7yy5hTgBRYUUzIjfdbGq3k1TWZQMl5UdJiSl4_zIjBtMmowt5hYrskbPDgblB9otEH1Zje_Kpg7HgoL9_ni0UyqNZZtV47XKuA_pZcdar3eHeKM7J6fVnN39Pl59ti_rRMW1blIWVMFEJ0VdlWdV2wpqspa0QNwGsslWZCd3WZI6dIGxRdzYDpUiuRc80BFJuRh-PYnbNf-3ibHIxvse_ViHbvJa9YRWsholAchfFK7x12cufMoNyPBCoPCOVWnhHKA0IJICOf2Hp_2rFvBtTnxhOzKHg-CjA--m3QSd8aHFvUxmEbpLbm_y1_QT6HIA</recordid><startdate>20050201</startdate><enddate>20050201</enddate><creator>Krumova, Sashka B.</creator><creator>Todinova, Svetla J.</creator><creator>Busheva, Mira C.</creator><creator>Taneva, Stefka G.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20050201</creationdate><title>Kinetic nature of the thermal destabilization of LHCII macroaggregates</title><author>Krumova, Sashka B. ; Todinova, Svetla J. ; Busheva, Mira C. ; Taneva, Stefka G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c372t-338488f75c79943bf903b891169e5ad38df952e60e0be8f9313d5da826d611a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Calorimetric enthalpy</topic><topic>Calorimetry, Differential Scanning</topic><topic>Denaturation transition</topic><topic>Differential scanning calorimetry</topic><topic>Enzyme Stability</topic><topic>Fluorescence emission</topic><topic>Kinetics</topic><topic>Light-harvesting chlorophyll a/b pigment–protein complex</topic><topic>Photosystem II Protein Complex - chemistry</topic><topic>Photosystem II Protein Complex - isolation & purification</topic><topic>Photosystem II Protein Complex - metabolism</topic><topic>Pisum sativum - enzymology</topic><topic>Protein Denaturation</topic><topic>Spectrometry, Fluorescence</topic><topic>Spinacia oleracea - enzymology</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Krumova, Sashka B.</creatorcontrib><creatorcontrib>Todinova, Svetla J.</creatorcontrib><creatorcontrib>Busheva, Mira C.</creatorcontrib><creatorcontrib>Taneva, Stefka G.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of photochemistry and photobiology. B, Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Krumova, Sashka B.</au><au>Todinova, Svetla J.</au><au>Busheva, Mira C.</au><au>Taneva, Stefka G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinetic nature of the thermal destabilization of LHCII macroaggregates</atitle><jtitle>Journal of photochemistry and photobiology. B, Biology</jtitle><addtitle>J Photochem Photobiol B</addtitle><date>2005-02-01</date><risdate>2005</risdate><volume>78</volume><issue>2</issue><spage>165</spage><epage>170</epage><pages>165-170</pages><issn>1011-1344</issn><eissn>1873-2682</eissn><abstract>The main light-harvesting chl
a/b pigment–protein complex of photosystem II (LHCII) in isolated state forms macroaggregates with different ultrastructure and lipid content [I. Simidjiev, V. Barzda, L. Mustardy, G. Garab, Anal. Biochem. 250 (1997) 169–175]. The thermodynamic stability of highly delipidated tightly bound LHCII macroaggregates is studied by differential scanning calorimetry and fluorescence spectroscopy. The calorimetric profile of LHCII is asymmetric, the denaturation transition is taking place at around 72 °C. A shoulder, which overlaps with the main denaturation transition, appears around 58 °C. The denaturation temperature strongly depends on the scanning rate indicating the kinetic nature of the thermal destabilization of LHCII macroaggregates. The fluorescence data prove that the thermal denaturation of LHCII is an irreversible and kinetically controlled process.</abstract><cop>Switzerland</cop><pub>Elsevier B.V</pub><pmid>15664504</pmid><doi>10.1016/j.jphotobiol.2004.11.005</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1011-1344 |
| ispartof | Journal of photochemistry and photobiology. B, Biology, 2005-02, Vol.78 (2), p.165-170 |
| issn | 1011-1344 1873-2682 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_67370988 |
| source | ScienceDirect Journals |
| subjects | Calorimetric enthalpy Calorimetry, Differential Scanning Denaturation transition Differential scanning calorimetry Enzyme Stability Fluorescence emission Kinetics Light-harvesting chlorophyll a/b pigment–protein complex Photosystem II Protein Complex - chemistry Photosystem II Protein Complex - isolation & purification Photosystem II Protein Complex - metabolism Pisum sativum - enzymology Protein Denaturation Spectrometry, Fluorescence Spinacia oleracea - enzymology Temperature |
| title | Kinetic nature of the thermal destabilization of LHCII macroaggregates |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T10%3A51%3A52IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Kinetic%20nature%20of%20the%20thermal%20destabilization%20of%20LHCII%20macroaggregates&rft.jtitle=Journal%20of%20photochemistry%20and%20photobiology.%20B,%20Biology&rft.au=Krumova,%20Sashka%20B.&rft.date=2005-02-01&rft.volume=78&rft.issue=2&rft.spage=165&rft.epage=170&rft.pages=165-170&rft.issn=1011-1344&rft.eissn=1873-2682&rft_id=info:doi/10.1016/j.jphotobiol.2004.11.005&rft_dat=%3Cproquest_cross%3E67370988%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c372t-338488f75c79943bf903b891169e5ad38df952e60e0be8f9313d5da826d611a3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=67370988&rft_id=info:pmid/15664504&rfr_iscdi=true |