Characterization and Postulated Structure of the Primary Emitter in the Bacterial Luciferase Reaction
An intermediate identifiable as the emitter in bacterial bioluminescence has been demonstrated. The reaction was carried out at 1 degrees C by mixing purified luciferasebound FMN 4a-hydroperoxide with long-chain aldehyde (decanal). Simultaneous kinetic measurements of bioluminescence and absorbance...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1984-05, Vol.81 (10), p.2990-2994 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Kurfürst, Manfred Ghisla, Sandro Hastings, J. Woodland |
| description | An intermediate identifiable as the emitter in bacterial bioluminescence has been demonstrated. The reaction was carried out at 1 degrees C by mixing purified luciferasebound FMN 4a-hydroperoxide with long-chain aldehyde (decanal). Simultaneous kinetic measurements of bioluminescence and absorbance showed that the decay of light emission occurred more rapidly than the appearance of the stable product, oxidized FMN, indicating the formation of a transient intermediate species subsequent to light emission. The same species was found in reaction mixtures examined immediately after light emission was completed. It has a relatively short half-life (7 min at 9 degrees C); the chromophore is postulated to be the luciferase-bound flavin 4a-hydroxide and to decay to the stable product, FMN, by losing water. Both its absorption spectrum (λmax, 360 nm) and its fluorescence emission (λmax, 490 nm) are consistent with the hypothesis that this is the ground state of the primary emitter, the bioluminescent species produced in the reaction. |
| doi_str_mv | 10.1073/pnas.81.10.2990 |
| format | Article |
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Woodland</creator><creatorcontrib>Kurfürst, Manfred ; Ghisla, Sandro ; Hastings, J. Woodland</creatorcontrib><description>An intermediate identifiable as the emitter in bacterial bioluminescence has been demonstrated. The reaction was carried out at 1 degrees C by mixing purified luciferasebound FMN 4a-hydroperoxide with long-chain aldehyde (decanal). Simultaneous kinetic measurements of bioluminescence and absorbance showed that the decay of light emission occurred more rapidly than the appearance of the stable product, oxidized FMN, indicating the formation of a transient intermediate species subsequent to light emission. The same species was found in reaction mixtures examined immediately after light emission was completed. It has a relatively short half-life (7 min at 9 degrees C); the chromophore is postulated to be the luciferase-bound flavin 4a-hydroxide and to decay to the stable product, FMN, by losing water. 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It has a relatively short half-life (7 min at 9 degrees C); the chromophore is postulated to be the luciferase-bound flavin 4a-hydroxide and to decay to the stable product, FMN, by losing water. Both its absorption spectrum (λmax, 360 nm) and its fluorescence emission (λmax, 490 nm) are consistent with the hypothesis that this is the ground state of the primary emitter, the bioluminescent species produced in the reaction.</description><subject>Absorption spectra</subject><subject>Aldehydes</subject><subject>Biochemistry</subject><subject>Biological Sciences: Biochemistry</subject><subject>Bioluminescence</subject><subject>Chromophores</subject><subject>Elution</subject><subject>Emission spectra</subject><subject>Fluorescence</subject><subject>Light emission</subject><subject>Visible spectrum</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><recordid>eNptkc1v1DAQxS0EokvhjMQB-cYpW3_Fjg8cYNUC0kpUfJytSTJhXWXjxXYQ8Nc3IUu7SJxGM_N7b0Z6hDznbM2ZkReHAdK64lOzFtayB2TFmeWFVpY9JCvGhCkqJdQZeZLSDWPMlhV7TM64Lq1UWqwIbnYQockY_W_IPgwUhpZeh5THHjK29HOOY5PHiDR0NO-QXke_h_iLXu59nmTUD3_GbxcT6Ol2bHyHERLSTzhNJ9On5FEHfcJnx3pOvl5dftm8L7Yf333YvNkWjdIyF0bxmtuq5thJEEy22hgAW3KhTKs6rDvVVlqUDKSwpkQtEFtVW6FA2qaR8py8XnwPY73HtsEhR-jdYXnZBfDu383gd-5b-OGkKgXTk_7VUR_D9xFTdnufGux7GDCMyRkptTLKVhN5sZBNDClF7O6OcObmaNwcjav43M_RTIqXp7_d88csTo7Pyr_rewfXjX2f8Wc-sfo_OQEvFuAm5RDvCCE1F_IWoiOtuQ</recordid><startdate>19840501</startdate><enddate>19840501</enddate><creator>Kurfürst, Manfred</creator><creator>Ghisla, Sandro</creator><creator>Hastings, J. 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Woodland</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c463t-741b198b1ef3a203d677aa951247d4febf4d86250a32975e62eed4b924a39cc33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Absorption spectra</topic><topic>Aldehydes</topic><topic>Biochemistry</topic><topic>Biological Sciences: Biochemistry</topic><topic>Bioluminescence</topic><topic>Chromophores</topic><topic>Elution</topic><topic>Emission spectra</topic><topic>Fluorescence</topic><topic>Light emission</topic><topic>Visible spectrum</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kurfürst, Manfred</creatorcontrib><creatorcontrib>Ghisla, Sandro</creatorcontrib><creatorcontrib>Hastings, J. 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Woodland</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization and Postulated Structure of the Primary Emitter in the Bacterial Luciferase Reaction</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1984-05-01</date><risdate>1984</risdate><volume>81</volume><issue>10</issue><spage>2990</spage><epage>2994</epage><pages>2990-2994</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>An intermediate identifiable as the emitter in bacterial bioluminescence has been demonstrated. The reaction was carried out at 1 degrees C by mixing purified luciferasebound FMN 4a-hydroperoxide with long-chain aldehyde (decanal). Simultaneous kinetic measurements of bioluminescence and absorbance showed that the decay of light emission occurred more rapidly than the appearance of the stable product, oxidized FMN, indicating the formation of a transient intermediate species subsequent to light emission. The same species was found in reaction mixtures examined immediately after light emission was completed. It has a relatively short half-life (7 min at 9 degrees C); the chromophore is postulated to be the luciferase-bound flavin 4a-hydroxide and to decay to the stable product, FMN, by losing water. Both its absorption spectrum (λmax, 360 nm) and its fluorescence emission (λmax, 490 nm) are consistent with the hypothesis that this is the ground state of the primary emitter, the bioluminescent species produced in the reaction.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>16593462</pmid><doi>10.1073/pnas.81.10.2990</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1984-05, Vol.81 (10), p.2990-2994 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pnas_primary_81_10_2990_fulltext |
| source | JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Absorption spectra Aldehydes Biochemistry Biological Sciences: Biochemistry Bioluminescence Chromophores Elution Emission spectra Fluorescence Light emission Visible spectrum |
| title | Characterization and Postulated Structure of the Primary Emitter in the Bacterial Luciferase Reaction |
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