Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima
Fe-only hydrogenases contain a di-iron active site complex, in which the two Fe atoms have carbon monoxide and cyanide ligands and are linked together by a putative di(thiomethyl)amine molecule. We have cloned, purified and characterized the HydE and HydG proteins, thought to be involved in the bios...
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| Veröffentlicht in: | FEBS letters 2005-09, Vol.579 (22), p.5055-5060 |
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| creator | Rubach, Jon K. Brazzolotto, Xavier Gaillard, Jacques Fontecave, Marc |
| description | Fe-only hydrogenases contain a di-iron active site complex, in which the two Fe atoms have carbon monoxide and cyanide ligands and are linked together by a putative di(thiomethyl)amine molecule. We have cloned, purified and characterized the HydE and HydG proteins, thought to be involved in the biosynthesis of this peculiar metal site, from the thermophilic organism
Thermotoga maritima. The HydE protein anaerobically reconstituted with iron and sulfide binds two [4Fe–4S] clusters, as characterized by UV and EPR spectroscopy. The HydG protein binds one [4Fe–4S] cluster, and probably an additional one. Both enzymes are able to reductively cleave
S-adenosylmethionine (SAM) when reduced by dithionite, confirming that they are Radical-SAM enzymes. |
| doi_str_mv | 10.1016/j.febslet.2005.07.092 |
| format | Article |
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Thermotoga maritima. The HydE protein anaerobically reconstituted with iron and sulfide binds two [4Fe–4S] clusters, as characterized by UV and EPR spectroscopy. The HydG protein binds one [4Fe–4S] cluster, and probably an additional one. Both enzymes are able to reductively cleave
S-adenosylmethionine (SAM) when reduced by dithionite, confirming that they are Radical-SAM enzymes.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2005.07.092</identifier><identifier>PMID: 16137685</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>1,4-dithio-d,l-threitol ; 5′-deoxyadenosine ; AdoH ; Amino Acid Sequence ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Binding Sites ; DTT ; Escherichia coli Proteins - metabolism ; Fe-only hydrogenase ; HydE ; HydG ; Hydrogenase - biosynthesis ; Hydrogenase - chemistry ; Hydrogenase - genetics ; IPTG ; Iron - metabolism ; Iron-Sulfur Proteins - biosynthesis ; Iron-Sulfur Proteins - chemistry ; Iron-Sulfur Proteins - genetics ; isopropyl-β-d-thiogalactopyranoside ; Maturation ; Molecular Sequence Data ; Molecular Structure ; Radical-SAM ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; S-adenosylmethionine ; S-Adenosylmethionine - metabolism ; SAM ; Sequence Alignment ; Sulfur - metabolism ; Sulfur donor ; Thermotoga maritima ; Thermotoga maritima - enzymology ; Trans-Activators - metabolism</subject><ispartof>FEBS letters, 2005-09, Vol.579 (22), p.5055-5060</ispartof><rights>2005 Federation of European Biochemical Societies</rights><rights>FEBS Letters 579 (2005) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5069-921c1b8bebc03b9bd03807b87fbc7c3ef2d420f3be66be16096e9d5055cd4e9a3</citedby><cites>FETCH-LOGICAL-c5069-921c1b8bebc03b9bd03807b87fbc7c3ef2d420f3be66be16096e9d5055cd4e9a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2005.07.092$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2005.07.092$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,778,782,1414,1430,3539,27911,27912,45561,45562,45982,46396,46820</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16137685$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rubach, Jon K.</creatorcontrib><creatorcontrib>Brazzolotto, Xavier</creatorcontrib><creatorcontrib>Gaillard, Jacques</creatorcontrib><creatorcontrib>Fontecave, Marc</creatorcontrib><title>Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Fe-only hydrogenases contain a di-iron active site complex, in which the two Fe atoms have carbon monoxide and cyanide ligands and are linked together by a putative di(thiomethyl)amine molecule. We have cloned, purified and characterized the HydE and HydG proteins, thought to be involved in the biosynthesis of this peculiar metal site, from the thermophilic organism
Thermotoga maritima. The HydE protein anaerobically reconstituted with iron and sulfide binds two [4Fe–4S] clusters, as characterized by UV and EPR spectroscopy. The HydG protein binds one [4Fe–4S] cluster, and probably an additional one. Both enzymes are able to reductively cleave
S-adenosylmethionine (SAM) when reduced by dithionite, confirming that they are Radical-SAM enzymes.</description><subject>1,4-dithio-d,l-threitol</subject><subject>5′-deoxyadenosine</subject><subject>AdoH</subject><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding Sites</subject><subject>DTT</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Fe-only hydrogenase</subject><subject>HydE</subject><subject>HydG</subject><subject>Hydrogenase - biosynthesis</subject><subject>Hydrogenase - chemistry</subject><subject>Hydrogenase - genetics</subject><subject>IPTG</subject><subject>Iron - metabolism</subject><subject>Iron-Sulfur Proteins - biosynthesis</subject><subject>Iron-Sulfur Proteins - chemistry</subject><subject>Iron-Sulfur Proteins - genetics</subject><subject>isopropyl-β-d-thiogalactopyranoside</subject><subject>Maturation</subject><subject>Molecular Sequence Data</subject><subject>Molecular Structure</subject><subject>Radical-SAM</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>S-adenosylmethionine</subject><subject>S-Adenosylmethionine - metabolism</subject><subject>SAM</subject><subject>Sequence Alignment</subject><subject>Sulfur - metabolism</subject><subject>Sulfur donor</subject><subject>Thermotoga maritima</subject><subject>Thermotoga maritima - enzymology</subject><subject>Trans-Activators - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1v1DAQhi0EokvhJ4B84pYwTtaJfUK02naRKnGgnC1_TLpeJXGxs0Xpr8dRVuJYTrblZ96x5yHkI4OSAWu-HMsOTepxKisAXkJbgqxekQ0TbV3U20a8JhsAti14K-sL8i6lI-SzYPItuWANq9tG8A1JVz7YAw7e6p7ag47aThj9s558GGno6HRAup_djurRLZtb6mMYizD2Mz3MLoYHHHVCOujpFNcqHJ_nARPtYhjo_QFjvgsPOiPRT37Q78mbTvcJP5zXS_LrZnd_vS_uftx-v_52V1gOjSxkxSwzwqCxUBtpHNQCWiPaztjW1thVbltBVxtsGoOsAdmgdBw4t26LUteX5POa-xjD7xOmSQ0-Wex7PWI4JZUHwBsuqhdBJluQUooM8hW0MaQUsVOPMX8ozoqBWrSoozprUYsWBa3KWnLdp3ODkxnQ_as6e8jAfgX--B7n_0tVN7ur6ufieFEMHEAKIXPU1zUK82ifPEaVrMfRovMR7aRc8C-89i-0WrkH</recordid><startdate>20050912</startdate><enddate>20050912</enddate><creator>Rubach, Jon K.</creator><creator>Brazzolotto, Xavier</creator><creator>Gaillard, Jacques</creator><creator>Fontecave, Marc</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20050912</creationdate><title>Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima</title><author>Rubach, Jon K. ; Brazzolotto, Xavier ; Gaillard, Jacques ; Fontecave, Marc</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5069-921c1b8bebc03b9bd03807b87fbc7c3ef2d420f3be66be16096e9d5055cd4e9a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>1,4-dithio-d,l-threitol</topic><topic>5′-deoxyadenosine</topic><topic>AdoH</topic><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Binding Sites</topic><topic>DTT</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Fe-only hydrogenase</topic><topic>HydE</topic><topic>HydG</topic><topic>Hydrogenase - biosynthesis</topic><topic>Hydrogenase - chemistry</topic><topic>Hydrogenase - genetics</topic><topic>IPTG</topic><topic>Iron - metabolism</topic><topic>Iron-Sulfur Proteins - biosynthesis</topic><topic>Iron-Sulfur Proteins - chemistry</topic><topic>Iron-Sulfur Proteins - genetics</topic><topic>isopropyl-β-d-thiogalactopyranoside</topic><topic>Maturation</topic><topic>Molecular Sequence Data</topic><topic>Molecular Structure</topic><topic>Radical-SAM</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>S-adenosylmethionine</topic><topic>S-Adenosylmethionine - metabolism</topic><topic>SAM</topic><topic>Sequence Alignment</topic><topic>Sulfur - metabolism</topic><topic>Sulfur donor</topic><topic>Thermotoga maritima</topic><topic>Thermotoga maritima - enzymology</topic><topic>Trans-Activators - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rubach, Jon K.</creatorcontrib><creatorcontrib>Brazzolotto, Xavier</creatorcontrib><creatorcontrib>Gaillard, Jacques</creatorcontrib><creatorcontrib>Fontecave, Marc</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rubach, Jon K.</au><au>Brazzolotto, Xavier</au><au>Gaillard, Jacques</au><au>Fontecave, Marc</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2005-09-12</date><risdate>2005</risdate><volume>579</volume><issue>22</issue><spage>5055</spage><epage>5060</epage><pages>5055-5060</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Fe-only hydrogenases contain a di-iron active site complex, in which the two Fe atoms have carbon monoxide and cyanide ligands and are linked together by a putative di(thiomethyl)amine molecule. We have cloned, purified and characterized the HydE and HydG proteins, thought to be involved in the biosynthesis of this peculiar metal site, from the thermophilic organism
Thermotoga maritima. The HydE protein anaerobically reconstituted with iron and sulfide binds two [4Fe–4S] clusters, as characterized by UV and EPR spectroscopy. The HydG protein binds one [4Fe–4S] cluster, and probably an additional one. Both enzymes are able to reductively cleave
S-adenosylmethionine (SAM) when reduced by dithionite, confirming that they are Radical-SAM enzymes.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>16137685</pmid><doi>10.1016/j.febslet.2005.07.092</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 1,4-dithio-d,l-threitol 5′-deoxyadenosine AdoH Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Binding Sites DTT Escherichia coli Proteins - metabolism Fe-only hydrogenase HydE HydG Hydrogenase - biosynthesis Hydrogenase - chemistry Hydrogenase - genetics IPTG Iron - metabolism Iron-Sulfur Proteins - biosynthesis Iron-Sulfur Proteins - chemistry Iron-Sulfur Proteins - genetics isopropyl-β-d-thiogalactopyranoside Maturation Molecular Sequence Data Molecular Structure Radical-SAM Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism S-adenosylmethionine S-Adenosylmethionine - metabolism SAM Sequence Alignment Sulfur - metabolism Sulfur donor Thermotoga maritima Thermotoga maritima - enzymology Trans-Activators - metabolism |
| title | Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima |
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