Membrane-bound flavin adenine dinucleotide in methanobacterium bryantii
Noncovalently attached flavin was isolated and partially purified from the membrane fraction of Methanobacterium Bryantii. The flavin was identified as FAD by absorption and fluorescence spectroscopy, effects on the spectra of reduction and of protonation, phenol extractability, behavior in thin lay...
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Veröffentlicht in: | Biochem. Biophys. Res. Commun.; (United States) 1981-05, Vol.100 (1), p.240-246 |
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description | Noncovalently attached flavin was isolated and partially purified from the membrane fraction of
Methanobacterium Bryantii. The flavin was identified as FAD by absorption and fluorescence spectroscopy, effects on the spectra of reduction and of protonation, phenol extractability, behavior in thin layer chromatography in two solvent systems, and ability to reconstitute activity of the FAD-specific enzyme D-amino acid oxidase. These singular organisms thus are capable of synthesizing isoalloxazine-type flavins as well as the unique 5-deazaflavin factor F
420. Membrane-bound FAD may thus (in addition to iron-sulfur centers and a nickel species) be involved in energy-coupled methanogenesis. |
doi_str_mv | 10.1016/S0006-291X(81)80088-5 |
format | Article |
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Methanobacterium Bryantii. The flavin was identified as FAD by absorption and fluorescence spectroscopy, effects on the spectra of reduction and of protonation, phenol extractability, behavior in thin layer chromatography in two solvent systems, and ability to reconstitute activity of the FAD-specific enzyme D-amino acid oxidase. These singular organisms thus are capable of synthesizing isoalloxazine-type flavins as well as the unique 5-deazaflavin factor F
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Methanobacterium Bryantii. The flavin was identified as FAD by absorption and fluorescence spectroscopy, effects on the spectra of reduction and of protonation, phenol extractability, behavior in thin layer chromatography in two solvent systems, and ability to reconstitute activity of the FAD-specific enzyme D-amino acid oxidase. These singular organisms thus are capable of synthesizing isoalloxazine-type flavins as well as the unique 5-deazaflavin factor F
420. Membrane-bound FAD may thus (in addition to iron-sulfur centers and a nickel species) be involved in energy-coupled methanogenesis.</description><subject>140505 - Solar Energy Conversion- Photochemical, Photobiological, & Thermochemical Conversion- (1980-)</subject><subject>550700 - Microbiology</subject><subject>ABSORPTION SPECTROSCOPY</subject><subject>BACTERIA</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Cell Membrane - analysis</subject><subject>CHROMATOGRAPHY</subject><subject>D-Amino-Acid Oxidase - metabolism</subject><subject>ELECTRON TRANSFER</subject><subject>EMISSION SPECTROSCOPY</subject><subject>ENZYME ACTIVITY</subject><subject>ENZYMES</subject><subject>Euryarchaeota - analysis</subject><subject>Flavin-Adenine Dinucleotide - analysis</subject><subject>FLUORESCENCE SPECTROSCOPY</subject><subject>HETEROCYCLIC COMPOUNDS</subject><subject>ISOALLOXAZINES</subject><subject>Kinetics</subject><subject>MEMBRANES</subject><subject>METHANOGENIC BACTERIA</subject><subject>MICROORGANISMS</subject><subject>ORGANIC COMPOUNDS</subject><subject>ORGANIC NITROGEN COMPOUNDS</subject><subject>ORGANIC OXYGEN COMPOUNDS</subject><subject>OXIDOREDUCTASES</subject><subject>SEPARATION PROCESSES</subject><subject>SOLAR ENERGY</subject><subject>SPECTRA</subject><subject>Spectrometry, Fluorescence</subject><subject>SPECTROSCOPY</subject><subject>THIN-LAYER CHROMATOGRAPHY</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtr3DAQgEVp2WweP2HB5FDSg9uRvZLlUwlLui2k9JAEchN6jIiKLaWSvJB_X292yTWnETPfaGY-QlYUvlKg_NsdAPC66enjlaBfBIAQNftAlhR6qBsK649k-YackNOc_wJQuub9giz4_Ojadkm2v3HUSQWsdZyCrdygdj5UymLwASvrw2QGjMVbrOb8iOVJhaiVKZj8NFY6vahQvD8nn5waMl4c4xl5-HFzv_lZ3_7Z_tpc39amFV2puaCKcdUbt-4RtNJGYNMJ2wBYhj12TjvVuI4qBabhfM2M09oy2imnaIvtGbk8_Btz8TIbX9A8mRgCmiJZA30HfIY-H6DnFP9NmIscfTY4DPOdccqya5ngXLQzyA6gSTHnhE4-Jz-q9CIpyL1l-WpZ7hVKQeWrZcnmvtVxwKRHtG9dR61z_fuhjrOKnce03xSDQevTflEb_TsT_gOhFI3H</recordid><startdate>19810515</startdate><enddate>19810515</enddate><creator>Lancaster, Jack R.</creator><general>Elsevier Inc</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>OTOTI</scope></search><sort><creationdate>19810515</creationdate><title>Membrane-bound flavin adenine dinucleotide in methanobacterium bryantii</title><author>Lancaster, Jack R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c387t-681a56a9cf49e0babc8e278d200d5e9e7fbfa2f71aa0c26645cfbbd517afa13e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>140505 - Solar Energy Conversion- Photochemical, Photobiological, & Thermochemical Conversion- (1980-)</topic><topic>550700 - Microbiology</topic><topic>ABSORPTION SPECTROSCOPY</topic><topic>BACTERIA</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>Cell Membrane - analysis</topic><topic>CHROMATOGRAPHY</topic><topic>D-Amino-Acid Oxidase - metabolism</topic><topic>ELECTRON TRANSFER</topic><topic>EMISSION SPECTROSCOPY</topic><topic>ENZYME ACTIVITY</topic><topic>ENZYMES</topic><topic>Euryarchaeota - analysis</topic><topic>Flavin-Adenine Dinucleotide - analysis</topic><topic>FLUORESCENCE SPECTROSCOPY</topic><topic>HETEROCYCLIC COMPOUNDS</topic><topic>ISOALLOXAZINES</topic><topic>Kinetics</topic><topic>MEMBRANES</topic><topic>METHANOGENIC BACTERIA</topic><topic>MICROORGANISMS</topic><topic>ORGANIC COMPOUNDS</topic><topic>ORGANIC NITROGEN COMPOUNDS</topic><topic>ORGANIC OXYGEN COMPOUNDS</topic><topic>OXIDOREDUCTASES</topic><topic>SEPARATION PROCESSES</topic><topic>SOLAR ENERGY</topic><topic>SPECTRA</topic><topic>Spectrometry, Fluorescence</topic><topic>SPECTROSCOPY</topic><topic>THIN-LAYER CHROMATOGRAPHY</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lancaster, Jack R.</creatorcontrib><creatorcontrib>Utah State Univ., Logan</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>OSTI.GOV</collection><jtitle>Biochem. Biophys. Res. Commun.; (United States)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lancaster, Jack R.</au><aucorp>Utah State Univ., Logan</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Membrane-bound flavin adenine dinucleotide in methanobacterium bryantii</atitle><jtitle>Biochem. Biophys. Res. Commun.; (United States)</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1981-05-15</date><risdate>1981</risdate><volume>100</volume><issue>1</issue><spage>240</spage><epage>246</epage><pages>240-246</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Noncovalently attached flavin was isolated and partially purified from the membrane fraction of
Methanobacterium Bryantii. The flavin was identified as FAD by absorption and fluorescence spectroscopy, effects on the spectra of reduction and of protonation, phenol extractability, behavior in thin layer chromatography in two solvent systems, and ability to reconstitute activity of the FAD-specific enzyme D-amino acid oxidase. These singular organisms thus are capable of synthesizing isoalloxazine-type flavins as well as the unique 5-deazaflavin factor F
420. Membrane-bound FAD may thus (in addition to iron-sulfur centers and a nickel species) be involved in energy-coupled methanogenesis.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>6114733</pmid><doi>10.1016/S0006-291X(81)80088-5</doi><tpages>7</tpages></addata></record> |
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subjects | 140505 - Solar Energy Conversion- Photochemical, Photobiological, & Thermochemical Conversion- (1980-) 550700 - Microbiology ABSORPTION SPECTROSCOPY BACTERIA BASIC BIOLOGICAL SCIENCES Cell Membrane - analysis CHROMATOGRAPHY D-Amino-Acid Oxidase - metabolism ELECTRON TRANSFER EMISSION SPECTROSCOPY ENZYME ACTIVITY ENZYMES Euryarchaeota - analysis Flavin-Adenine Dinucleotide - analysis FLUORESCENCE SPECTROSCOPY HETEROCYCLIC COMPOUNDS ISOALLOXAZINES Kinetics MEMBRANES METHANOGENIC BACTERIA MICROORGANISMS ORGANIC COMPOUNDS ORGANIC NITROGEN COMPOUNDS ORGANIC OXYGEN COMPOUNDS OXIDOREDUCTASES SEPARATION PROCESSES SOLAR ENERGY SPECTRA Spectrometry, Fluorescence SPECTROSCOPY THIN-LAYER CHROMATOGRAPHY |
title | Membrane-bound flavin adenine dinucleotide in methanobacterium bryantii |
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