The iron-sulfur centers of the soluble [NiFeSe] hydrogenase, from Desulfovibrio baculatus (DSM 1743) : EPR and Mössbauer characterization
The soluble (cytoplasmic plus periplasmic) Ni/Fe-S/Se-containing hydrogenase from Desulfovibrio baculatus (DSM 1743) was purified from cells grown in an 57Fe-enriched medium, and its iron-sulfur centers were extensively characterized by Mössbauer and EPR spectroscopies. The data analysis excludes th...
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| Veröffentlicht in: | European journal of biochemistry 1990-04, Vol.189 (2), p.381-386 |
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| container_title | European journal of biochemistry |
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| creator | TEIXEIRA, M MOURA, I FAUQUE, G DERVARTANIAN, D. V LEGALL, J PECK, H. D. JR MOURA, J. J. G HUYNH, B. H |
| description | The soluble (cytoplasmic plus periplasmic) Ni/Fe-S/Se-containing hydrogenase from Desulfovibrio baculatus (DSM 1743) was purified from cells grown in an 57Fe-enriched medium, and its iron-sulfur centers were extensively characterized by Mössbauer and EPR spectroscopies. The data analysis excludes the presence of a [3Fe-4S] center, either in the native (as isolated) or in the hydrogen-reduced states. In the native state, the non-heme iron atoms are arranged as two diamagnetic [4Fe-4S]2+ centers. Upon reduction, these two centers exhibit distinct and unusual Mössbauer spectroscopic parameters. The centers were found to have similar mid-point potentials (approximately -315 mV) as determined by oxidation-reduction titratins followed by EPR. |
| doi_str_mv | 10.1111/j.1432-1033.1990.tb15499.x |
| format | Article |
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The centers were found to have similar mid-point potentials (approximately -315 mV) as determined by oxidation-reduction titratins followed by EPR.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1990.tb15499.x</identifier><identifier>PMID: 2159882</identifier><identifier>CODEN: EJBCAI</identifier><language>eng</language><publisher>Oxford: Blackwell</publisher><subject>Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Desulfovibrio - enzymology ; Electron Spin Resonance Spectroscopy - methods ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Hydrogenase - isolation & purification ; Hydrogenase - metabolism ; Iron-Sulfur Proteins - isolation & purification ; Iron-Sulfur Proteins - metabolism ; Macromolecular Substances ; Metalloproteins - metabolism ; Nickel - analysis ; Oxidoreductases ; Protein Conformation ; Selenium - analysis ; Spectrum Analysis - methods</subject><ispartof>European journal of biochemistry, 1990-04, Vol.189 (2), p.381-386</ispartof><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c286t-6b8fe7e0e5cafe7a60188c809d0c6581526415f181fc7f7c8a3887faa8d84cf03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6886803$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2159882$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>TEIXEIRA, M</creatorcontrib><creatorcontrib>MOURA, I</creatorcontrib><creatorcontrib>FAUQUE, G</creatorcontrib><creatorcontrib>DERVARTANIAN, D. 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Upon reduction, these two centers exhibit distinct and unusual Mössbauer spectroscopic parameters. The centers were found to have similar mid-point potentials (approximately -315 mV) as determined by oxidation-reduction titratins followed by EPR.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Desulfovibrio - enzymology</subject><subject>Electron Spin Resonance Spectroscopy - methods</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogenase - isolation & purification</subject><subject>Hydrogenase - metabolism</subject><subject>Iron-Sulfur Proteins - isolation & purification</subject><subject>Iron-Sulfur Proteins - metabolism</subject><subject>Macromolecular Substances</subject><subject>Metalloproteins - metabolism</subject><subject>Nickel - analysis</subject><subject>Oxidoreductases</subject><subject>Protein Conformation</subject><subject>Selenium - analysis</subject><subject>Spectrum Analysis - methods</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9Ue1qFTEUDKLUa_URhCAiFdw12Y9s0n-lXwqtiq2_RMLZ7Il3L3s3NdlI6yP4QH0BX8wsXe75cw7MzBmYIeQVZzlP836T86osMs7KMudKsXxqeV0pld8-Iqsd9JisGONVVqhaPCXPQtgwxoQSzR7ZK3itpCxW5O_1Gmnv3ZiFONjoqcFxQh-os3RKUHBDbAek3z_1Z3iFP-j6rvPuJ44Q8B213m3pCc5S97tvfe9oCyYOMMVAD06uLilvqvItPaSnX75SGDt6-e8-hBYiJqc1eDDJrP8DU-_G5-SJhSHgi2Xvk29np9fHH7KLz-cfj48uMlNIMWWilRYbZFgbSAcIxqU0kqmOGVFLXhei4rXlklvT2MZIKKVsLIDsZGUsK_fJm4e_N979ihgmve2DwWGAEV0MulGNqMpGJuLhA9F4F4JHq298vwV_pznTcxF6o-e09Zy2novQSxH6NolfLi6x3WK3ky7JJ_z1gkMwMFgPo-nDjiakFDK9_Q-FrpPU</recordid><startdate>19900430</startdate><enddate>19900430</enddate><creator>TEIXEIRA, M</creator><creator>MOURA, I</creator><creator>FAUQUE, G</creator><creator>DERVARTANIAN, D. 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H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c286t-6b8fe7e0e5cafe7a60188c809d0c6581526415f181fc7f7c8a3887faa8d84cf03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Desulfovibrio - enzymology</topic><topic>Electron Spin Resonance Spectroscopy - methods</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogenase - isolation & purification</topic><topic>Hydrogenase - metabolism</topic><topic>Iron-Sulfur Proteins - isolation & purification</topic><topic>Iron-Sulfur Proteins - metabolism</topic><topic>Macromolecular Substances</topic><topic>Metalloproteins - metabolism</topic><topic>Nickel - analysis</topic><topic>Oxidoreductases</topic><topic>Protein Conformation</topic><topic>Selenium - analysis</topic><topic>Spectrum Analysis - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>TEIXEIRA, M</creatorcontrib><creatorcontrib>MOURA, I</creatorcontrib><creatorcontrib>FAUQUE, G</creatorcontrib><creatorcontrib>DERVARTANIAN, D. V</creatorcontrib><creatorcontrib>LEGALL, J</creatorcontrib><creatorcontrib>PECK, H. D. JR</creatorcontrib><creatorcontrib>MOURA, J. J. G</creatorcontrib><creatorcontrib>HUYNH, B. 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H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The iron-sulfur centers of the soluble [NiFeSe] hydrogenase, from Desulfovibrio baculatus (DSM 1743) : EPR and Mössbauer characterization</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1990-04-30</date><risdate>1990</risdate><volume>189</volume><issue>2</issue><spage>381</spage><epage>386</epage><pages>381-386</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>The soluble (cytoplasmic plus periplasmic) Ni/Fe-S/Se-containing hydrogenase from Desulfovibrio baculatus (DSM 1743) was purified from cells grown in an 57Fe-enriched medium, and its iron-sulfur centers were extensively characterized by Mössbauer and EPR spectroscopies. The data analysis excludes the presence of a [3Fe-4S] center, either in the native (as isolated) or in the hydrogen-reduced states. In the native state, the non-heme iron atoms are arranged as two diamagnetic [4Fe-4S]2+ centers. Upon reduction, these two centers exhibit distinct and unusual Mössbauer spectroscopic parameters. The centers were found to have similar mid-point potentials (approximately -315 mV) as determined by oxidation-reduction titratins followed by EPR.</abstract><cop>Oxford</cop><pub>Blackwell</pub><pmid>2159882</pmid><doi>10.1111/j.1432-1033.1990.tb15499.x</doi><tpages>6</tpages></addata></record> |
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| ispartof | European journal of biochemistry, 1990-04, Vol.189 (2), p.381-386 |
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| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Desulfovibrio - enzymology Electron Spin Resonance Spectroscopy - methods Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrogenase - isolation & purification Hydrogenase - metabolism Iron-Sulfur Proteins - isolation & purification Iron-Sulfur Proteins - metabolism Macromolecular Substances Metalloproteins - metabolism Nickel - analysis Oxidoreductases Protein Conformation Selenium - analysis Spectrum Analysis - methods |
| title | The iron-sulfur centers of the soluble [NiFeSe] hydrogenase, from Desulfovibrio baculatus (DSM 1743) : EPR and Mössbauer characterization |
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