Trace cobalt speciation in bacteria and at enzymic active sites using emission Mössbauer spectroscopy
57Co emission Mössbauer spectroscopy (EMS) allows the chemical state of cobalt, as influenced by its coordination environment, to be monitored in biological samples at its physiological (trace) concentrations. To draw attention to EMS as a valuable tool for speciation of cobalt in biocomplexes, the...
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Veröffentlicht in: | Analytical and bioanalytical chemistry 2002-02, Vol.372 (3), p.431-435 |
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creator | Kamnev, A A Antonyuk, L P Smirnova, V E Serebrennikova, O B Kulikov, L A Perfiliev, Yu D |
description | 57Co emission Mössbauer spectroscopy (EMS) allows the chemical state of cobalt, as influenced by its coordination environment, to be monitored in biological samples at its physiological (trace) concentrations. To draw attention to EMS as a valuable tool for speciation of cobalt in biocomplexes, the process of cobalt(II) metabolism in cells of the plant growth-promoting rhizobacterium Azospirillum brasilense Sp245 was investigated using EMS of 57CoII-doped bacterial cells. EMS measurements also showed 57CoII-activated glutamine synthetase (GS, a key enzyme of nitrogen metabolism, isolated from this bacterium) to have two different cobalt(II) forms at its active sites, in agreement with data available on other bacterial GSs. Chemical after-effects following electron capture by the nucleus of the parent 57CoII during the 57Co-->57Fe transition, which contribute to the formation of a stabilised daughter 57FeIII component along with the nucleogenic 57FeII forms, are also briefly considered. |
doi_str_mv | 10.1007/s00216-001-1116-7 |
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To draw attention to EMS as a valuable tool for speciation of cobalt in biocomplexes, the process of cobalt(II) metabolism in cells of the plant growth-promoting rhizobacterium Azospirillum brasilense Sp245 was investigated using EMS of 57CoII-doped bacterial cells. EMS measurements also showed 57CoII-activated glutamine synthetase (GS, a key enzyme of nitrogen metabolism, isolated from this bacterium) to have two different cobalt(II) forms at its active sites, in agreement with data available on other bacterial GSs. 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Chemical after-effects following electron capture by the nucleus of the parent 57CoII during the 57Co-->57Fe transition, which contribute to the formation of a stabilised daughter 57FeIII component along with the nucleogenic 57FeII forms, are also briefly considered.</description><subject>Azospirillum brasilense - enzymology</subject><subject>Binding Sites</subject><subject>Cobalt - analysis</subject><subject>Cobalt - metabolism</subject><subject>Glutamate-Ammonia Ligase - metabolism</subject><subject>Spectroscopy, Mossbauer</subject><subject>Trace Elements</subject><issn>1618-2642</issn><issn>1618-2650</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkMtOwzAQRS0EoqXwAWyQV-wCfiRxvEQVL6mITVlbtjNBRnlhO0jlw_gBfgyXVrCa0ejeqzsHoXNKrigh4joQwmiZEUIzStMiDtCclrTKWFmQw789ZzN0EsJb0hUVLY_RjFLJZcHkHDVrry1gOxjdRhxGsE5HN_TY9dhoG8E7jXVfYx0x9J-bzlmczu4DcHARAp6C618xdC6Ere3p-ysEoyfwv2HRD8EO4-YUHTW6DXC2nwv0cne7Xj5kq-f7x-XNKrNMiphJKQ2wugJZpnZ5RZtC1FIYy3NuZa2Z1MZCTSA9wAzTghFW61xQbnJpGecLdLnLHf3wPkGIKhWz0La6h2EKSiQChDOahHQntKlh8NCo0btO-42iRG3hqh1claCpLVwlkudiHz6ZDup_x54m_wHt33cG</recordid><startdate>20020201</startdate><enddate>20020201</enddate><creator>Kamnev, A A</creator><creator>Antonyuk, L P</creator><creator>Smirnova, V E</creator><creator>Serebrennikova, O B</creator><creator>Kulikov, L A</creator><creator>Perfiliev, Yu D</creator><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>20020201</creationdate><title>Trace cobalt speciation in bacteria and at enzymic active sites using emission Mössbauer spectroscopy</title><author>Kamnev, A A ; Antonyuk, L P ; Smirnova, V E ; Serebrennikova, O B ; Kulikov, L A ; Perfiliev, Yu D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c297t-999be2d8e96529481f57d97bc343c9da29abced0e1192b2a7202da4713b49c233</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Azospirillum brasilense - enzymology</topic><topic>Binding Sites</topic><topic>Cobalt - analysis</topic><topic>Cobalt - metabolism</topic><topic>Glutamate-Ammonia Ligase - metabolism</topic><topic>Spectroscopy, Mossbauer</topic><topic>Trace Elements</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kamnev, A A</creatorcontrib><creatorcontrib>Antonyuk, L P</creatorcontrib><creatorcontrib>Smirnova, V E</creatorcontrib><creatorcontrib>Serebrennikova, O B</creatorcontrib><creatorcontrib>Kulikov, L A</creatorcontrib><creatorcontrib>Perfiliev, Yu D</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><jtitle>Analytical and bioanalytical chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kamnev, A A</au><au>Antonyuk, L P</au><au>Smirnova, V E</au><au>Serebrennikova, O B</au><au>Kulikov, L A</au><au>Perfiliev, Yu D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Trace cobalt speciation in bacteria and at enzymic active sites using emission Mössbauer spectroscopy</atitle><jtitle>Analytical and bioanalytical chemistry</jtitle><addtitle>Anal Bioanal Chem</addtitle><date>2002-02-01</date><risdate>2002</risdate><volume>372</volume><issue>3</issue><spage>431</spage><epage>435</epage><pages>431-435</pages><issn>1618-2642</issn><eissn>1618-2650</eissn><abstract>57Co emission Mössbauer spectroscopy (EMS) allows the chemical state of cobalt, as influenced by its coordination environment, to be monitored in biological samples at its physiological (trace) concentrations. To draw attention to EMS as a valuable tool for speciation of cobalt in biocomplexes, the process of cobalt(II) metabolism in cells of the plant growth-promoting rhizobacterium Azospirillum brasilense Sp245 was investigated using EMS of 57CoII-doped bacterial cells. EMS measurements also showed 57CoII-activated glutamine synthetase (GS, a key enzyme of nitrogen metabolism, isolated from this bacterium) to have two different cobalt(II) forms at its active sites, in agreement with data available on other bacterial GSs. Chemical after-effects following electron capture by the nucleus of the parent 57CoII during the 57Co-->57Fe transition, which contribute to the formation of a stabilised daughter 57FeIII component along with the nucleogenic 57FeII forms, are also briefly considered.</abstract><cop>Germany</cop><pmid>11939529</pmid><doi>10.1007/s00216-001-1116-7</doi><tpages>5</tpages></addata></record> |
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subjects | Azospirillum brasilense - enzymology Binding Sites Cobalt - analysis Cobalt - metabolism Glutamate-Ammonia Ligase - metabolism Spectroscopy, Mossbauer Trace Elements |
title | Trace cobalt speciation in bacteria and at enzymic active sites using emission Mössbauer spectroscopy |
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