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Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase
The fluorescence signal of the single tryptophan residue (Trp 69) of Fusarium solani pisi cutinase is highly quenched. However, prolonged irradiation of the enzyme in the tryptophan absorption band causes an increase of the tryptophan fluorescence quantum yield by an order of magnitude. By using a c...
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| Published in: | FEBS letters 1999-08, Vol.456 (3), p.409-416 |
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| Main Authors: | , , |
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| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c4264-def61056858e2324bf905ec951ee36567a1fffe3e17d1b092e8192b12b0efa8d3 |
| container_end_page | 416 |
| container_issue | 3 |
| container_start_page | 409 |
| container_title | FEBS letters |
| container_volume | 456 |
| creator | Prompers, Jeanine J. Hilbers, Cornelis W. Pepermans, Henri A.M. |
| description | The fluorescence signal of the single tryptophan residue (Trp
69) of
Fusarium solani pisi cutinase is highly quenched. However, prolonged irradiation of the enzyme in the tryptophan absorption band causes an increase of the tryptophan fluorescence quantum yield by an order of magnitude. By using a combination of NMR spectroscopy and chemical detection of free thiol groups with a sulfhydryl reagent we could unambiguously show that the unusual fluorescence behaviour of Trp
69 in cutinase is caused by the breaking of the disulfide bond between Cys
31 and Cys
109 upon irradiation, while the amide-aromatic hydrogen bond between Ala
32 and Trp
69 remains intact. This is the first example of tryptophan mediated photoreduction of a disulfide bond in proteins. |
| doi_str_mv | 10.1016/S0014-5793(99)00990-4 |
| format | article |
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69) of
Fusarium solani pisi cutinase is highly quenched. However, prolonged irradiation of the enzyme in the tryptophan absorption band causes an increase of the tryptophan fluorescence quantum yield by an order of magnitude. By using a combination of NMR spectroscopy and chemical detection of free thiol groups with a sulfhydryl reagent we could unambiguously show that the unusual fluorescence behaviour of Trp
69 in cutinase is caused by the breaking of the disulfide bond between Cys
31 and Cys
109 upon irradiation, while the amide-aromatic hydrogen bond between Ala
32 and Trp
69 remains intact. This is the first example of tryptophan mediated photoreduction of a disulfide bond in proteins.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(99)00990-4</identifier><identifier>PMID: 10462054</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Alanine - chemistry ; Amides - chemistry ; Carboxylic Ester Hydrolases - chemistry ; Carboxylic Ester Hydrolases - radiation effects ; CSA, chemical shift anisotropy ; Cutinase ; Cysteine - chemistry ; Disulfide bond ; Disulfides - chemistry ; DTNB, 5,5′-dithiobis(2-nitrobenzoic acid) ; FHSQC, fast HSQC ; Fluorescence ; Fluorescence spectroscopy ; Fusarium - enzymology ; HSQC, heteronuclear single-quantum coherence spectroscopy ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy - methods ; Nitrogen Isotopes ; NMR, nuclear magnetic resonance ; NOE, nuclear Overhauser effect ; NOESY, nuclear Overhauser enhancement spectroscopy ; Nuclear magnetic resonance ; Sulfhydryl Compounds - chemistry ; Sulfhydryl Reagents - chemistry ; Thiol ; TOCSY, total correlation spectroscopy ; TPPI, time proportional phase incrementation ; Tryptophan - chemistry ; Tryptophan - radiation effects ; Tryptophan mediated photoreduction</subject><ispartof>FEBS letters, 1999-08, Vol.456 (3), p.409-416</ispartof><rights>1999 Federation of European Biochemical Societies</rights><rights>FEBS Letters 456 (1999) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4264-def61056858e2324bf905ec951ee36567a1fffe3e17d1b092e8192b12b0efa8d3</citedby><cites>FETCH-LOGICAL-c4264-def61056858e2324bf905ec951ee36567a1fffe3e17d1b092e8192b12b0efa8d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579399009904$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3549,27924,27925,45780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10462054$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Prompers, Jeanine J.</creatorcontrib><creatorcontrib>Hilbers, Cornelis W.</creatorcontrib><creatorcontrib>Pepermans, Henri A.M.</creatorcontrib><title>Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The fluorescence signal of the single tryptophan residue (Trp
69) of
Fusarium solani pisi cutinase is highly quenched. However, prolonged irradiation of the enzyme in the tryptophan absorption band causes an increase of the tryptophan fluorescence quantum yield by an order of magnitude. By using a combination of NMR spectroscopy and chemical detection of free thiol groups with a sulfhydryl reagent we could unambiguously show that the unusual fluorescence behaviour of Trp
69 in cutinase is caused by the breaking of the disulfide bond between Cys
31 and Cys
109 upon irradiation, while the amide-aromatic hydrogen bond between Ala
32 and Trp
69 remains intact. This is the first example of tryptophan mediated photoreduction of a disulfide bond in proteins.</description><subject>Alanine - chemistry</subject><subject>Amides - chemistry</subject><subject>Carboxylic Ester Hydrolases - chemistry</subject><subject>Carboxylic Ester Hydrolases - radiation effects</subject><subject>CSA, chemical shift anisotropy</subject><subject>Cutinase</subject><subject>Cysteine - chemistry</subject><subject>Disulfide bond</subject><subject>Disulfides - chemistry</subject><subject>DTNB, 5,5′-dithiobis(2-nitrobenzoic acid)</subject><subject>FHSQC, fast HSQC</subject><subject>Fluorescence</subject><subject>Fluorescence spectroscopy</subject><subject>Fusarium - enzymology</subject><subject>HSQC, heteronuclear single-quantum coherence spectroscopy</subject><subject>Hydrogen Bonding</subject><subject>Magnetic Resonance Spectroscopy - methods</subject><subject>Nitrogen Isotopes</subject><subject>NMR, nuclear magnetic resonance</subject><subject>NOE, nuclear Overhauser effect</subject><subject>NOESY, nuclear Overhauser enhancement spectroscopy</subject><subject>Nuclear magnetic resonance</subject><subject>Sulfhydryl Compounds - chemistry</subject><subject>Sulfhydryl Reagents - chemistry</subject><subject>Thiol</subject><subject>TOCSY, total correlation spectroscopy</subject><subject>TPPI, time proportional phase incrementation</subject><subject>Tryptophan - chemistry</subject><subject>Tryptophan - radiation effects</subject><subject>Tryptophan mediated photoreduction</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNqNkEFv3CAUhFHUKtmk_QmpOFXNwS3YwJpTlUbZpFKkHpqeEYaHlshrXDCpVvnzxeso6i09Id6bGYYPoXNKPlNCxZefhFBW8bVsPkl5QYiUpGJHaEXbdVM1TLRv0OpFcoJOU3og5d5SeYxOKGGiJpyt0NN93I9TGLd6wDuwXk9g8bgNU4hgs5l8GHBw2PqUe-ct4C4MFhudEySch5yy7rHrc5EnA4MpAtjqRx9ynH2bnHT0eYdT6PXg8eiTxyZPftAJ3qG3TvcJ3j-fZ-jX5vr-6ra6-3Hz_eryrjKsFqyy4AQlXLS8hbqpWeck4WAkpwCN4GKtqXMOGqBrSzsiayifrDtadwScbm1zhj4uuWMMvzOkSe18KduXRhByUkLK4hC8CPkiNDGkFMGpMfqdjntFiZqpqwN1NSNVUqoDdcWK78PzA7krEP9xLZiL4HYR_PE97P8vVW2uv9WHzbwoo3k8R31doqAQe_QQVTJ-Bm99BDMpG_wrbf8CoZ6pDQ</recordid><startdate>19990813</startdate><enddate>19990813</enddate><creator>Prompers, Jeanine J.</creator><creator>Hilbers, Cornelis W.</creator><creator>Pepermans, Henri A.M.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><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>19990813</creationdate><title>Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase</title><author>Prompers, Jeanine J. ; Hilbers, Cornelis W. ; Pepermans, Henri A.M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4264-def61056858e2324bf905ec951ee36567a1fffe3e17d1b092e8192b12b0efa8d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Alanine - chemistry</topic><topic>Amides - chemistry</topic><topic>Carboxylic Ester Hydrolases - chemistry</topic><topic>Carboxylic Ester Hydrolases - radiation effects</topic><topic>CSA, chemical shift anisotropy</topic><topic>Cutinase</topic><topic>Cysteine - chemistry</topic><topic>Disulfide bond</topic><topic>Disulfides - chemistry</topic><topic>DTNB, 5,5′-dithiobis(2-nitrobenzoic acid)</topic><topic>FHSQC, fast HSQC</topic><topic>Fluorescence</topic><topic>Fluorescence spectroscopy</topic><topic>Fusarium - enzymology</topic><topic>HSQC, heteronuclear single-quantum coherence spectroscopy</topic><topic>Hydrogen Bonding</topic><topic>Magnetic Resonance Spectroscopy - methods</topic><topic>Nitrogen Isotopes</topic><topic>NMR, nuclear magnetic resonance</topic><topic>NOE, nuclear Overhauser effect</topic><topic>NOESY, nuclear Overhauser enhancement spectroscopy</topic><topic>Nuclear magnetic resonance</topic><topic>Sulfhydryl Compounds - chemistry</topic><topic>Sulfhydryl Reagents - chemistry</topic><topic>Thiol</topic><topic>TOCSY, total correlation spectroscopy</topic><topic>TPPI, time proportional phase incrementation</topic><topic>Tryptophan - chemistry</topic><topic>Tryptophan - radiation effects</topic><topic>Tryptophan mediated photoreduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Prompers, Jeanine J.</creatorcontrib><creatorcontrib>Hilbers, Cornelis W.</creatorcontrib><creatorcontrib>Pepermans, Henri A.M.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Prompers, Jeanine J.</au><au>Hilbers, Cornelis W.</au><au>Pepermans, Henri A.M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1999-08-13</date><risdate>1999</risdate><volume>456</volume><issue>3</issue><spage>409</spage><epage>416</epage><pages>409-416</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The fluorescence signal of the single tryptophan residue (Trp
69) of
Fusarium solani pisi cutinase is highly quenched. However, prolonged irradiation of the enzyme in the tryptophan absorption band causes an increase of the tryptophan fluorescence quantum yield by an order of magnitude. By using a combination of NMR spectroscopy and chemical detection of free thiol groups with a sulfhydryl reagent we could unambiguously show that the unusual fluorescence behaviour of Trp
69 in cutinase is caused by the breaking of the disulfide bond between Cys
31 and Cys
109 upon irradiation, while the amide-aromatic hydrogen bond between Ala
32 and Trp
69 remains intact. This is the first example of tryptophan mediated photoreduction of a disulfide bond in proteins.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>10462054</pmid><doi>10.1016/S0014-5793(99)00990-4</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1999-08, Vol.456 (3), p.409-416 |
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| language | eng |
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| source | Wiley; ScienceDirect Journals |
| subjects | Alanine - chemistry Amides - chemistry Carboxylic Ester Hydrolases - chemistry Carboxylic Ester Hydrolases - radiation effects CSA, chemical shift anisotropy Cutinase Cysteine - chemistry Disulfide bond Disulfides - chemistry DTNB, 5,5′-dithiobis(2-nitrobenzoic acid) FHSQC, fast HSQC Fluorescence Fluorescence spectroscopy Fusarium - enzymology HSQC, heteronuclear single-quantum coherence spectroscopy Hydrogen Bonding Magnetic Resonance Spectroscopy - methods Nitrogen Isotopes NMR, nuclear magnetic resonance NOE, nuclear Overhauser effect NOESY, nuclear Overhauser enhancement spectroscopy Nuclear magnetic resonance Sulfhydryl Compounds - chemistry Sulfhydryl Reagents - chemistry Thiol TOCSY, total correlation spectroscopy TPPI, time proportional phase incrementation Tryptophan - chemistry Tryptophan - radiation effects Tryptophan mediated photoreduction |
| title | Tryptophan mediated photoreduction of disulfide bond causes unusual fluorescence behaviour of Fusarium solani pisi cutinase |
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