Fluorescence Quenching Study on the Interaction between Quercetin and Lipoxygenase
The interaction between quercetin and lipoxygenase was investigated by fluorescence spectroscopy. The analysis of the emission quenching at different temperatures revealed that the quenching mechanism correspond to a static process and, as consequence, a complex quercetin-lipoxygenase is formed. The...
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| Veröffentlicht in: | Journal of fluorescence 2011-05, Vol.21 (3), p.1311-1318 |
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| container_title | Journal of fluorescence |
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| creator | Pinto, María del Carmen Duque, Antonio Luis Macías, Pedro |
| description | The interaction between quercetin and lipoxygenase was investigated by fluorescence spectroscopy. The analysis of the emission quenching at different temperatures revealed that the quenching mechanism correspond to a static process and, as consequence, a complex quercetin-lipoxygenase is formed. The thermodynamic parameters
ΔG
,
ΔH
and
ΔS
were calculated to be−32.57 kJmol
−1
,−3.21 kJmol
−1
and 87.14 Jmol
−1
K
−1
respectively, which suggest that hydrophobic forces plays a major role in the stabilization of the complex quercetin-lipoxygenase. The distance, r, between donor (lipoxygenase) and acceptor (quercetin) was calculated to be 3.84 nm based on Förster’s non-radiative energy transfer theory. The results obtained from the evaluation of three dimensional florescence spectra suggest a conformational modification of the protein in the region of the coupling with quercetin. |
| doi_str_mv | 10.1007/s10895-010-0816-9 |
| format | Article |
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ΔG
,
ΔH
and
ΔS
were calculated to be−32.57 kJmol
−1
,−3.21 kJmol
−1
and 87.14 Jmol
−1
K
−1
respectively, which suggest that hydrophobic forces plays a major role in the stabilization of the complex quercetin-lipoxygenase. The distance, r, between donor (lipoxygenase) and acceptor (quercetin) was calculated to be 3.84 nm based on Förster’s non-radiative energy transfer theory. The results obtained from the evaluation of three dimensional florescence spectra suggest a conformational modification of the protein in the region of the coupling with quercetin.</description><identifier>ISSN: 1053-0509</identifier><identifier>EISSN: 1573-4994</identifier><identifier>DOI: 10.1007/s10895-010-0816-9</identifier><identifier>PMID: 21222146</identifier><language>eng</language><publisher>Boston: Springer US</publisher><subject>Analytical Chemistry ; Beryllium ; Biochemistry ; Biological and Medical Physics ; Biomedical and Life Sciences ; Biomedicine ; Biophysics ; Biotechnology ; Energy Transfer ; Fluorescence ; Fluorescence Resonance Energy Transfer ; Hydrophobic and Hydrophilic Interactions ; Lipoxygenase ; Lipoxygenase - chemistry ; Mathematical analysis ; Original Paper ; Protein Binding ; Protein Conformation ; Quenching ; Quercetin - chemistry ; Spectra ; Spectrometry, Fluorescence ; Stabilization ; Temperature ; Thermodynamics</subject><ispartof>Journal of fluorescence, 2011-05, Vol.21 (3), p.1311-1318</ispartof><rights>Springer Science+Business Media, LLC 2011</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-7da8c726ecabeaf130ccd4a9d00c5b54464244a3d3b3e806b40e83b2d3f22e4f3</citedby><cites>FETCH-LOGICAL-c375t-7da8c726ecabeaf130ccd4a9d00c5b54464244a3d3b3e806b40e83b2d3f22e4f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10895-010-0816-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10895-010-0816-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21222146$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pinto, María del Carmen</creatorcontrib><creatorcontrib>Duque, Antonio Luis</creatorcontrib><creatorcontrib>Macías, Pedro</creatorcontrib><title>Fluorescence Quenching Study on the Interaction between Quercetin and Lipoxygenase</title><title>Journal of fluorescence</title><addtitle>J Fluoresc</addtitle><addtitle>J Fluoresc</addtitle><description>The interaction between quercetin and lipoxygenase was investigated by fluorescence spectroscopy. The analysis of the emission quenching at different temperatures revealed that the quenching mechanism correspond to a static process and, as consequence, a complex quercetin-lipoxygenase is formed. The thermodynamic parameters
ΔG
,
ΔH
and
ΔS
were calculated to be−32.57 kJmol
−1
,−3.21 kJmol
−1
and 87.14 Jmol
−1
K
−1
respectively, which suggest that hydrophobic forces plays a major role in the stabilization of the complex quercetin-lipoxygenase. The distance, r, between donor (lipoxygenase) and acceptor (quercetin) was calculated to be 3.84 nm based on Förster’s non-radiative energy transfer theory. The results obtained from the evaluation of three dimensional florescence spectra suggest a conformational modification of the protein in the region of the coupling with quercetin.</description><subject>Analytical Chemistry</subject><subject>Beryllium</subject><subject>Biochemistry</subject><subject>Biological and Medical Physics</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Biophysics</subject><subject>Biotechnology</subject><subject>Energy Transfer</subject><subject>Fluorescence</subject><subject>Fluorescence Resonance Energy Transfer</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Lipoxygenase</subject><subject>Lipoxygenase - chemistry</subject><subject>Mathematical analysis</subject><subject>Original Paper</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Quenching</subject><subject>Quercetin - chemistry</subject><subject>Spectra</subject><subject>Spectrometry, Fluorescence</subject><subject>Stabilization</subject><subject>Temperature</subject><subject>Thermodynamics</subject><issn>1053-0509</issn><issn>1573-4994</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtOwzAQRS0EouXxAWxQdqwC40die4kqCkiVEK-15TiTEtQ6xU4E_XtctbCE1cxozlxpDiFnFC4pgLyKFJQucqCQg6JlrvfImBaS50JrsZ96KHgOBegROYrxHQC0EuqQjBhljFFRjsnTdDF0AaND7zB7HFJ5a_08e-6Hep11PuvfMLv3PQbr-jbNFfafiH6DBod96zPr62zWrrqv9Ry9jXhCDhq7iHi6q8fkdXrzMrnLZw-395PrWe64LPpc1lY5yUp0tkLbUA7O1cLqGsAVVSFEKZgQlte84qigrASg4hWrecMYioYfk4tt7ip0HwPG3izb9MdiYT12QzSalZwpmXz8RyrJJUhgPJF0S7rQxRiwMavQLm1YGwpm49xsnZvk3GycG51uznfpQ7XE-vfiR3IC2BaIaeXnGMx7NwSf3PyR-g1CJY0B</recordid><startdate>20110501</startdate><enddate>20110501</enddate><creator>Pinto, María del Carmen</creator><creator>Duque, Antonio Luis</creator><creator>Macías, Pedro</creator><general>Springer US</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><scope>7U5</scope><scope>8FD</scope><scope>L7M</scope></search><sort><creationdate>20110501</creationdate><title>Fluorescence Quenching Study on the Interaction between Quercetin and Lipoxygenase</title><author>Pinto, María del Carmen ; Duque, Antonio Luis ; Macías, Pedro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-7da8c726ecabeaf130ccd4a9d00c5b54464244a3d3b3e806b40e83b2d3f22e4f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Analytical Chemistry</topic><topic>Beryllium</topic><topic>Biochemistry</topic><topic>Biological and Medical Physics</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Biophysics</topic><topic>Biotechnology</topic><topic>Energy Transfer</topic><topic>Fluorescence</topic><topic>Fluorescence Resonance Energy Transfer</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Lipoxygenase</topic><topic>Lipoxygenase - chemistry</topic><topic>Mathematical analysis</topic><topic>Original Paper</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Quenching</topic><topic>Quercetin - chemistry</topic><topic>Spectra</topic><topic>Spectrometry, Fluorescence</topic><topic>Stabilization</topic><topic>Temperature</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pinto, María del Carmen</creatorcontrib><creatorcontrib>Duque, Antonio Luis</creatorcontrib><creatorcontrib>Macías, Pedro</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><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Journal of fluorescence</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pinto, María del Carmen</au><au>Duque, Antonio Luis</au><au>Macías, Pedro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fluorescence Quenching Study on the Interaction between Quercetin and Lipoxygenase</atitle><jtitle>Journal of fluorescence</jtitle><stitle>J Fluoresc</stitle><addtitle>J Fluoresc</addtitle><date>2011-05-01</date><risdate>2011</risdate><volume>21</volume><issue>3</issue><spage>1311</spage><epage>1318</epage><pages>1311-1318</pages><issn>1053-0509</issn><eissn>1573-4994</eissn><abstract>The interaction between quercetin and lipoxygenase was investigated by fluorescence spectroscopy. The analysis of the emission quenching at different temperatures revealed that the quenching mechanism correspond to a static process and, as consequence, a complex quercetin-lipoxygenase is formed. The thermodynamic parameters
ΔG
,
ΔH
and
ΔS
were calculated to be−32.57 kJmol
−1
,−3.21 kJmol
−1
and 87.14 Jmol
−1
K
−1
respectively, which suggest that hydrophobic forces plays a major role in the stabilization of the complex quercetin-lipoxygenase. The distance, r, between donor (lipoxygenase) and acceptor (quercetin) was calculated to be 3.84 nm based on Förster’s non-radiative energy transfer theory. The results obtained from the evaluation of three dimensional florescence spectra suggest a conformational modification of the protein in the region of the coupling with quercetin.</abstract><cop>Boston</cop><pub>Springer US</pub><pmid>21222146</pmid><doi>10.1007/s10895-010-0816-9</doi><tpages>8</tpages></addata></record> |
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| subjects | Analytical Chemistry Beryllium Biochemistry Biological and Medical Physics Biomedical and Life Sciences Biomedicine Biophysics Biotechnology Energy Transfer Fluorescence Fluorescence Resonance Energy Transfer Hydrophobic and Hydrophilic Interactions Lipoxygenase Lipoxygenase - chemistry Mathematical analysis Original Paper Protein Binding Protein Conformation Quenching Quercetin - chemistry Spectra Spectrometry, Fluorescence Stabilization Temperature Thermodynamics |
| title | Fluorescence Quenching Study on the Interaction between Quercetin and Lipoxygenase |
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