Radical SAM-Dependent Carbon Insertion into the Nitrogenase M-Cluster
The active site of nitrogenase, the M-cluster, is a metal-sulfur cluster containing a carbide at its core. Using radiolabeling experiments, we show that this carbide originates from the methyl group of S-adenosylmethionine (SAM) and that it is inserted into the M-cluster by the assembly protein NifB...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2012-09, Vol.337 (6102), p.1672-1675 |
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| creator | Wiig, Jared A. Hu, Yilin Lee, Chi Chung Ribbe, Markus W. |
| description | The active site of nitrogenase, the M-cluster, is a metal-sulfur cluster containing a carbide at its core. Using radiolabeling experiments, we show that this carbide originates from the methyl group of S-adenosylmethionine (SAM) and that it is inserted into the M-cluster by the assembly protein NifB. Our SAM cleavage and deuterium substitution analyses suggest a similarity between the mechanism of carbon insertion by NifB and the proposed mechanism of RNA methylation by the radical SAM enzymes RlmN and Cfr, which involves methyl transfer from one SAM equivalent, followed by hydrogen atom abstraction from the methyl group by a 5'-deoxyadenosyl radical generated from a second SAM equivalent. This work is an initial step toward unraveling the importance of the interstitial carbide and providing insights into the nitrogenase mechanism. |
| doi_str_mv | 10.1126/science.1224603 |
| format | Article |
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Using radiolabeling experiments, we show that this carbide originates from the methyl group of S-adenosylmethionine (SAM) and that it is inserted into the M-cluster by the assembly protein NifB. Our SAM cleavage and deuterium substitution analyses suggest a similarity between the mechanism of carbon insertion by NifB and the proposed mechanism of RNA methylation by the radical SAM enzymes RlmN and Cfr, which involves methyl transfer from one SAM equivalent, followed by hydrogen atom abstraction from the methyl group by a 5'-deoxyadenosyl radical generated from a second SAM equivalent. This work is an initial step toward unraveling the importance of the interstitial carbide and providing insights into the nitrogenase mechanism.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1224603</identifier><identifier>PMID: 23019652</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Association for the Advancement of Science</publisher><subject>Aluminum ; ammonia ; Analytical, structural and metabolic biochemistry ; Atoms ; Bacteria ; Bacterial Proteins - chemistry ; Biological and medical sciences ; Carbides ; Carbon ; Carbon - chemistry ; Catalysis ; Catalytic Domain ; Deuterium ; Deuterium Exchange Measurement ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Hydrogen ; Insertion ; Ligands ; Metal clusters ; Methylation ; Methyltransferases - chemistry ; Molecular and cellular biology ; Nitrogen ; nitrogen cycle ; nitrogenase ; Nitrogenase - chemistry ; Radicals ; Radioactive decay ; Radiocarbon ; Resins ; Resultants ; RNA - chemistry ; S-adenosylmethionine ; S-Adenosylmethionine - chemistry</subject><ispartof>Science (American Association for the Advancement of Science), 2012-09, Vol.337 (6102), p.1672-1675</ispartof><rights>Copyright © 2012 American Association for the Advancement of Science</rights><rights>2014 INIST-CNRS</rights><rights>Copyright © 2012, American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c539t-c76cd27a10ef1178aeaa7195622ddfe3311fcdd7ec458d3a2c18a6b7559e571d3</citedby><cites>FETCH-LOGICAL-c539t-c76cd27a10ef1178aeaa7195622ddfe3311fcdd7ec458d3a2c18a6b7559e571d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41703619$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41703619$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,2871,2872,27903,27904,57995,58228</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26403869$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23019652$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wiig, Jared A.</creatorcontrib><creatorcontrib>Hu, Yilin</creatorcontrib><creatorcontrib>Lee, Chi Chung</creatorcontrib><creatorcontrib>Ribbe, Markus W.</creatorcontrib><title>Radical SAM-Dependent Carbon Insertion into the Nitrogenase M-Cluster</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>The active site of nitrogenase, the M-cluster, is a metal-sulfur cluster containing a carbide at its core. Using radiolabeling experiments, we show that this carbide originates from the methyl group of S-adenosylmethionine (SAM) and that it is inserted into the M-cluster by the assembly protein NifB. Our SAM cleavage and deuterium substitution analyses suggest a similarity between the mechanism of carbon insertion by NifB and the proposed mechanism of RNA methylation by the radical SAM enzymes RlmN and Cfr, which involves methyl transfer from one SAM equivalent, followed by hydrogen atom abstraction from the methyl group by a 5'-deoxyadenosyl radical generated from a second SAM equivalent. This work is an initial step toward unraveling the importance of the interstitial carbide and providing insights into the nitrogenase mechanism.</description><subject>Aluminum</subject><subject>ammonia</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Atoms</subject><subject>Bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Biological and medical sciences</subject><subject>Carbides</subject><subject>Carbon</subject><subject>Carbon - chemistry</subject><subject>Catalysis</subject><subject>Catalytic Domain</subject><subject>Deuterium</subject><subject>Deuterium Exchange Measurement</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen</subject><subject>Insertion</subject><subject>Ligands</subject><subject>Metal clusters</subject><subject>Methylation</subject><subject>Methyltransferases - chemistry</subject><subject>Molecular and cellular biology</subject><subject>Nitrogen</subject><subject>nitrogen cycle</subject><subject>nitrogenase</subject><subject>Nitrogenase - chemistry</subject><subject>Radicals</subject><subject>Radioactive decay</subject><subject>Radiocarbon</subject><subject>Resins</subject><subject>Resultants</subject><subject>RNA - chemistry</subject><subject>S-adenosylmethionine</subject><subject>S-Adenosylmethionine - chemistry</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c9rFDEUB_Agil2rZ0_KgBS8TJuXTJLJRSjbqoVWwR_nkE3etFlmM9tkRvC_N8Ou649LTwm8Tx5570vIS6CnAEyeZRcwOjwFxhpJ-SOyAKpFrRnlj8mCUi7rlipxRJ7lvKa01DR_So4Yp6ClYAty-cX64GxffT2_qS9wi9FjHKulTashVlcxYxpDuYU4DtV4h9WnMKbhFqPNWN3Uy37KI6bn5Eln-4wv9ucx-f7-8tvyY339-cPV8vy6doLrsXZKOs-UBYodgGotWqtAC8mY9x1yDtA57xW6RrSeW-agtXKlhNAoFHh-TN7t-m6n1Qa9K19NtjfbFDY2_TSDDebfSgx35nb4YXjLZSOa0uDtvkEa7ifMo9mE7LDvbcRhyobReWcAWj9IoaUtUCk1PEyLbHhLKSv0zX90PUwplqXNimqmlOZFne2US0POCbvDiEDNHLzZB2_2wZcXr__ezMH_TrqAkz2wueTdJRtdyH-cbChv5Tz2q51b53FIh3oDal6M5r8AWGm_tg</recordid><startdate>20120928</startdate><enddate>20120928</enddate><creator>Wiig, Jared A.</creator><creator>Hu, Yilin</creator><creator>Lee, Chi Chung</creator><creator>Ribbe, Markus W.</creator><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</general><scope>IQODW</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>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20120928</creationdate><title>Radical SAM-Dependent Carbon Insertion into the Nitrogenase M-Cluster</title><author>Wiig, Jared A. ; Hu, Yilin ; Lee, Chi Chung ; Ribbe, Markus W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c539t-c76cd27a10ef1178aeaa7195622ddfe3311fcdd7ec458d3a2c18a6b7559e571d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Aluminum</topic><topic>ammonia</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Atoms</topic><topic>Bacteria</topic><topic>Bacterial Proteins - chemistry</topic><topic>Biological and medical sciences</topic><topic>Carbides</topic><topic>Carbon</topic><topic>Carbon - chemistry</topic><topic>Catalysis</topic><topic>Catalytic Domain</topic><topic>Deuterium</topic><topic>Deuterium Exchange Measurement</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen</topic><topic>Insertion</topic><topic>Ligands</topic><topic>Metal clusters</topic><topic>Methylation</topic><topic>Methyltransferases - chemistry</topic><topic>Molecular and cellular biology</topic><topic>Nitrogen</topic><topic>nitrogen cycle</topic><topic>nitrogenase</topic><topic>Nitrogenase - chemistry</topic><topic>Radicals</topic><topic>Radioactive decay</topic><topic>Radiocarbon</topic><topic>Resins</topic><topic>Resultants</topic><topic>RNA - chemistry</topic><topic>S-adenosylmethionine</topic><topic>S-Adenosylmethionine - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wiig, Jared A.</creatorcontrib><creatorcontrib>Hu, Yilin</creatorcontrib><creatorcontrib>Lee, Chi Chung</creatorcontrib><creatorcontrib>Ribbe, Markus W.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wiig, Jared A.</au><au>Hu, Yilin</au><au>Lee, Chi Chung</au><au>Ribbe, Markus W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Radical SAM-Dependent Carbon Insertion into the Nitrogenase M-Cluster</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2012-09-28</date><risdate>2012</risdate><volume>337</volume><issue>6102</issue><spage>1672</spage><epage>1675</epage><pages>1672-1675</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>The active site of nitrogenase, the M-cluster, is a metal-sulfur cluster containing a carbide at its core. Using radiolabeling experiments, we show that this carbide originates from the methyl group of S-adenosylmethionine (SAM) and that it is inserted into the M-cluster by the assembly protein NifB. Our SAM cleavage and deuterium substitution analyses suggest a similarity between the mechanism of carbon insertion by NifB and the proposed mechanism of RNA methylation by the radical SAM enzymes RlmN and Cfr, which involves methyl transfer from one SAM equivalent, followed by hydrogen atom abstraction from the methyl group by a 5'-deoxyadenosyl radical generated from a second SAM equivalent. This work is an initial step toward unraveling the importance of the interstitial carbide and providing insights into the nitrogenase mechanism.</abstract><cop>Washington, DC</cop><pub>American Association for the Advancement of Science</pub><pmid>23019652</pmid><doi>10.1126/science.1224603</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Aluminum ammonia Analytical, structural and metabolic biochemistry Atoms Bacteria Bacterial Proteins - chemistry Biological and medical sciences Carbides Carbon Carbon - chemistry Catalysis Catalytic Domain Deuterium Deuterium Exchange Measurement Enzymes Fundamental and applied biological sciences. Psychology Hydrogen Insertion Ligands Metal clusters Methylation Methyltransferases - chemistry Molecular and cellular biology Nitrogen nitrogen cycle nitrogenase Nitrogenase - chemistry Radicals Radioactive decay Radiocarbon Resins Resultants RNA - chemistry S-adenosylmethionine S-Adenosylmethionine - chemistry |
| title | Radical SAM-Dependent Carbon Insertion into the Nitrogenase M-Cluster |
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