Triplet-Triplet Energy Transfer in α -Trypsin
Experiments are reported that demonstrate that light absorbed by ionized tyrosinyl sensitizes the phosphorescence of tryptophanyl residues of native α -tripsin. The sensitization effect is abolished when α -tripsin is unfolded in guanidine hydrochloride. Under the experimental conditions used, the t...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1973-12, Vol.70 (12), p.3703-3706 |
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| container_issue | 12 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 70 |
| creator | Ghiron, C. A. Longworth, J. W. Ramachandran, N. |
| description | Experiments are reported that demonstrate that light absorbed by ionized tyrosinyl sensitizes the phosphorescence of tryptophanyl residues of native α -tripsin. The sensitization effect is abolished when α -tripsin is unfolded in guanidine hydrochloride. Under the experimental conditions used, the tryptophan phosphorescence could only have been induced by an electron-exchange interaction. These results, therefore, require that there be at least one ionized tyrosinyl-tryptophanyl pair in the native enzyme and that the distance between the two side chains be sufficiently short to permit electron exchange. |
| doi_str_mv | 10.1073/pnas.70.12.3703 |
| format | Article |
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A. ; Longworth, J. W. ; Ramachandran, N.</creator><creatorcontrib>Ghiron, C. A. ; Longworth, J. W. ; Ramachandran, N.</creatorcontrib><description>Experiments are reported that demonstrate that light absorbed by ionized tyrosinyl sensitizes the phosphorescence of tryptophanyl residues of native α -tripsin. The sensitization effect is abolished when α -tripsin is unfolded in guanidine hydrochloride. Under the experimental conditions used, the tryptophan phosphorescence could only have been induced by an electron-exchange interaction. These results, therefore, require that there be at least one ionized tyrosinyl-tryptophanyl pair in the native enzyme and that the distance between the two side chains be sufficiently short to permit electron exchange.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.70.12.3703</identifier><identifier>PMID: 4521197</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amidines ; Biochemistry ; Biological Sciences: Biochemistry ; Cyclohexanecarboxylic Acids ; Emission spectra ; Energy Transfer ; Enzymes ; Fluorescence ; Guanidines ; Hydrogen-Ion Concentration ; Indoles ; Phosphorescence ; Protein Conformation ; Protein Denaturation ; Spectrometry, Fluorescence ; Time dependence ; Trypsin ; Trypsin Inhibitors ; Tryptophan ; Tyrosine ; Wavelengths</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1973-12, Vol.70 (12), p.3703-3706</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c461t-854af61ab35ed50ac8761155f36f0cd6de1543bb3d2ac0c85d2ca8be1f9b50cb3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/70/12.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/62631$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/62631$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,728,781,785,804,886,27928,27929,53795,53797,58021,58254</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4521197$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ghiron, C. A.</creatorcontrib><creatorcontrib>Longworth, J. W.</creatorcontrib><creatorcontrib>Ramachandran, N.</creatorcontrib><title>Triplet-Triplet Energy Transfer in α -Trypsin</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Experiments are reported that demonstrate that light absorbed by ionized tyrosinyl sensitizes the phosphorescence of tryptophanyl residues of native α -tripsin. The sensitization effect is abolished when α -tripsin is unfolded in guanidine hydrochloride. Under the experimental conditions used, the tryptophan phosphorescence could only have been induced by an electron-exchange interaction. These results, therefore, require that there be at least one ionized tyrosinyl-tryptophanyl pair in the native enzyme and that the distance between the two side chains be sufficiently short to permit electron exchange.</description><subject>Amidines</subject><subject>Biochemistry</subject><subject>Biological Sciences: Biochemistry</subject><subject>Cyclohexanecarboxylic Acids</subject><subject>Emission spectra</subject><subject>Energy Transfer</subject><subject>Enzymes</subject><subject>Fluorescence</subject><subject>Guanidines</subject><subject>Hydrogen-Ion Concentration</subject><subject>Indoles</subject><subject>Phosphorescence</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>Spectrometry, Fluorescence</subject><subject>Time dependence</subject><subject>Trypsin</subject><subject>Trypsin Inhibitors</subject><subject>Tryptophan</subject><subject>Tyrosine</subject><subject>Wavelengths</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kL1OwzAURi0EKqUwIyGBMsGU9l47dpKBAVXlR6rEUmbLcZwSlCbBThF9LF6EZyJRQ0UXpqurc75r6yPkHGGMELJJXSo3DtuFjlkI7IAMEWL0RRDDIRkC0NCPAhockxPn3gAg5hEMyCDgFDEOh2S8sHldmMbvpzcrjV1uvIVVpcuM9fLS-_7yWrypXV6ekqNMFc6c9XNEXu5ni-mjP39-eJrezX0dCGz8iAcqE6gSxk3KQekoFIicZ0xkoFORGuQBSxKWUqVBRzylWkWJwSxOOOiEjcjt9m69TlYm1aZsrCpkbfOVshtZqVzukzJ_lcvqQwY0ZAht_rrP2-p9bVwjV7nTpihUaaq1kxFFHqFgrTjZitpWzlmT7d5AkF3DsmtYhu1CZddwm7j8-7Wd31fa8qued8Ffunfg5l9BZuuiaMxn05oXW_PNNZXdqYIKhuwHekyZmQ</recordid><startdate>19731201</startdate><enddate>19731201</enddate><creator>Ghiron, C. A.</creator><creator>Longworth, J. W.</creator><creator>Ramachandran, N.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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>5PM</scope></search><sort><creationdate>19731201</creationdate><title>Triplet-Triplet Energy Transfer in α -Trypsin</title><author>Ghiron, C. A. ; Longworth, J. W. ; Ramachandran, N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c461t-854af61ab35ed50ac8761155f36f0cd6de1543bb3d2ac0c85d2ca8be1f9b50cb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>Amidines</topic><topic>Biochemistry</topic><topic>Biological Sciences: Biochemistry</topic><topic>Cyclohexanecarboxylic Acids</topic><topic>Emission spectra</topic><topic>Energy Transfer</topic><topic>Enzymes</topic><topic>Fluorescence</topic><topic>Guanidines</topic><topic>Hydrogen-Ion Concentration</topic><topic>Indoles</topic><topic>Phosphorescence</topic><topic>Protein Conformation</topic><topic>Protein Denaturation</topic><topic>Spectrometry, Fluorescence</topic><topic>Time dependence</topic><topic>Trypsin</topic><topic>Trypsin Inhibitors</topic><topic>Tryptophan</topic><topic>Tyrosine</topic><topic>Wavelengths</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ghiron, C. A.</creatorcontrib><creatorcontrib>Longworth, J. W.</creatorcontrib><creatorcontrib>Ramachandran, N.</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>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ghiron, C. A.</au><au>Longworth, J. W.</au><au>Ramachandran, N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Triplet-Triplet Energy Transfer in α -Trypsin</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1973-12-01</date><risdate>1973</risdate><volume>70</volume><issue>12</issue><spage>3703</spage><epage>3706</epage><pages>3703-3706</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Experiments are reported that demonstrate that light absorbed by ionized tyrosinyl sensitizes the phosphorescence of tryptophanyl residues of native α -tripsin. The sensitization effect is abolished when α -tripsin is unfolded in guanidine hydrochloride. Under the experimental conditions used, the tryptophan phosphorescence could only have been induced by an electron-exchange interaction. These results, therefore, require that there be at least one ionized tyrosinyl-tryptophanyl pair in the native enzyme and that the distance between the two side chains be sufficiently short to permit electron exchange.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>4521197</pmid><doi>10.1073/pnas.70.12.3703</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1973-12, Vol.70 (12), p.3703-3706 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_427310 |
| source | MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; JSTOR |
| subjects | Amidines Biochemistry Biological Sciences: Biochemistry Cyclohexanecarboxylic Acids Emission spectra Energy Transfer Enzymes Fluorescence Guanidines Hydrogen-Ion Concentration Indoles Phosphorescence Protein Conformation Protein Denaturation Spectrometry, Fluorescence Time dependence Trypsin Trypsin Inhibitors Tryptophan Tyrosine Wavelengths |
| title | Triplet-Triplet Energy Transfer in α -Trypsin |
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