X-ray Emission Spectroscopy Evidences a Central Carbon in the Nitrogenase Iron-Molybdenum Cofactor
Nitrogenase is a complex enzyme that catalyzes the reduction of dinitrogen to ammonia. Despite insight from structural and biochemical studies, its structure and mechanism await full characterization. An iron-molybdenum cofactor (FeMoco) is thought to be the site of dinitrogen reduction, but the ide...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2011-11, Vol.334 (6058), p.974-977 |
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| creator | Lancaster, Kyle M. Roemelt, Michael Ettenhuber, Patrick Hu, Yilin Ribbe, Markus W. Neese, Frank Bergmann, Uwe DeBeer, Serena |
| description | Nitrogenase is a complex enzyme that catalyzes the reduction of dinitrogen to ammonia. Despite insight from structural and biochemical studies, its structure and mechanism await full characterization. An iron-molybdenum cofactor (FeMoco) is thought to be the site of dinitrogen reduction, but the identity of a central atom in this cofactor remains unknown. Fe Kβ x-ray emission spectroscopy (XES) of intact nitrogenase MoFe protein, isolated FeMoco, and the FeMoco-deficient ΔnifB protein indicates that among the candidate atoms oxygen, nitrogen, and carbon, it is carbon that best fits the XES data. The experimental XES is supported by computational efforts, which show that oxidation and spin states do not affect the assignment of the central atom to C⁴⁺. Identification of the central atom will drive further studies on its role in catalysis. |
| doi_str_mv | 10.1126/science.1206445 |
| format | Article |
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Despite insight from structural and biochemical studies, its structure and mechanism await full characterization. An iron-molybdenum cofactor (FeMoco) is thought to be the site of dinitrogen reduction, but the identity of a central atom in this cofactor remains unknown. Fe Kβ x-ray emission spectroscopy (XES) of intact nitrogenase MoFe protein, isolated FeMoco, and the FeMoco-deficient ΔnifB protein indicates that among the candidate atoms oxygen, nitrogen, and carbon, it is carbon that best fits the XES data. The experimental XES is supported by computational efforts, which show that oxidation and spin states do not affect the assignment of the central atom to C⁴⁺. Identification of the central atom will drive further studies on its role in catalysis.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1206445</identifier><identifier>PMID: 22096198</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Association for the Advancement of Science</publisher><subject>Ammonia ; Analytical, structural and metabolic biochemistry ; Artificial satellites ; Atoms ; Azotobacter vinelandii - chemistry ; Biocatalysis ; Biochemistry ; Biological and medical sciences ; Carbon ; Carbon - chemistry ; catalytic activity ; Electrons ; Emission spectroscopy ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Infrared spectroscopy ; Iron ; Ligands ; Models, Molecular ; Molecular Structure ; Molybdoferredoxin - chemistry ; Molybdoferredoxin - metabolism ; Nitrogen ; Nitrogen - chemistry ; nitrogenase ; Oxidation ; Oxidation-Reduction ; Oxidoreductases ; oxygen ; Oxygen - chemistry ; Proteins ; Reduction ; Spectrometry, X-Ray Emission ; Spectroscopy ; X ray spectroscopy ; X-rays</subject><ispartof>Science (American Association for the Advancement of Science), 2011-11, Vol.334 (6058), p.974-977</ispartof><rights>Copyright © 2011 American Association for the Advancement of Science</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2011, American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c602t-e8afe27967b048e462824e88effe8e664aaed1c9d155c7aa8fc57e619cdf615d3</citedby><cites>FETCH-LOGICAL-c602t-e8afe27967b048e462824e88effe8e664aaed1c9d155c7aa8fc57e619cdf615d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41351746$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41351746$$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=24818145$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22096198$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lancaster, Kyle M.</creatorcontrib><creatorcontrib>Roemelt, Michael</creatorcontrib><creatorcontrib>Ettenhuber, Patrick</creatorcontrib><creatorcontrib>Hu, Yilin</creatorcontrib><creatorcontrib>Ribbe, Markus W.</creatorcontrib><creatorcontrib>Neese, Frank</creatorcontrib><creatorcontrib>Bergmann, Uwe</creatorcontrib><creatorcontrib>DeBeer, Serena</creatorcontrib><title>X-ray Emission Spectroscopy Evidences a Central Carbon in the Nitrogenase Iron-Molybdenum Cofactor</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Nitrogenase is a complex enzyme that catalyzes the reduction of dinitrogen to ammonia. Despite insight from structural and biochemical studies, its structure and mechanism await full characterization. An iron-molybdenum cofactor (FeMoco) is thought to be the site of dinitrogen reduction, but the identity of a central atom in this cofactor remains unknown. Fe Kβ x-ray emission spectroscopy (XES) of intact nitrogenase MoFe protein, isolated FeMoco, and the FeMoco-deficient ΔnifB protein indicates that among the candidate atoms oxygen, nitrogen, and carbon, it is carbon that best fits the XES data. The experimental XES is supported by computational efforts, which show that oxidation and spin states do not affect the assignment of the central atom to C⁴⁺. Identification of the central atom will drive further studies on its role in catalysis.</description><subject>Ammonia</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Artificial satellites</subject><subject>Atoms</subject><subject>Azotobacter vinelandii - chemistry</subject><subject>Biocatalysis</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Carbon</subject><subject>Carbon - chemistry</subject><subject>catalytic activity</subject><subject>Electrons</subject><subject>Emission spectroscopy</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Infrared spectroscopy</subject><subject>Iron</subject><subject>Ligands</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>Molybdoferredoxin - chemistry</subject><subject>Molybdoferredoxin - metabolism</subject><subject>Nitrogen</subject><subject>Nitrogen - chemistry</subject><subject>nitrogenase</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases</subject><subject>oxygen</subject><subject>Oxygen - chemistry</subject><subject>Proteins</subject><subject>Reduction</subject><subject>Spectrometry, X-Ray Emission</subject><subject>Spectroscopy</subject><subject>X ray spectroscopy</subject><subject>X-rays</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkkFv1DAQhS0EosvCmRMoQkJwSWs7tmNfkFDUQqUCB0DiZjnOpPUqay92Umn_fb3dsLQ9wMmS55unmTcPoZcEHxNCxUmyDryFY0KxYIw_QguCFS8VxdVjtMC4EqXENT9Cz1JaYZxrqnqKjijFShAlF6j9VUazLU7XLiUXfPF9A3aMIdmwyb_XrtvJp8IUDfgxmqFoTGwz53wxXkHx1WX4ErxJUJzH4MsvYdi2uWlaF03ojR1DfI6e9GZI8GJ-l-jn2emP5nN58e3TefPxorQC07EEaXqgtRJ1i5kEJqikDKSEvgcJQjBjoCNWdYRzWxsje8tryFvYrheEd9USfdjrbqZ2DZ3dD6w30a1N3OpgnL5f8e5KX4ZrXUmMRS2zwLtZIIbfE6RRZ1csDIPxEKaklaikIIKp_5OYi5pKzDP5_p8kxbsj1YqwjL55gK7CFH22TCsqFa1UHmCJTvaQzUdKEfrDfgTrXST0HAk9RyJ3vL5ry4H_k4EMvJ0Bk6wZ-mi8dekvxySR5Fbo1Z5bpXzVQ52RipOaieoG8jLK-Q</recordid><startdate>20111118</startdate><enddate>20111118</enddate><creator>Lancaster, Kyle M.</creator><creator>Roemelt, Michael</creator><creator>Ettenhuber, Patrick</creator><creator>Hu, Yilin</creator><creator>Ribbe, Markus W.</creator><creator>Neese, Frank</creator><creator>Bergmann, Uwe</creator><creator>DeBeer, Serena</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>7S9</scope><scope>L.6</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20111118</creationdate><title>X-ray Emission Spectroscopy Evidences a Central Carbon in the Nitrogenase Iron-Molybdenum Cofactor</title><author>Lancaster, Kyle M. ; Roemelt, Michael ; Ettenhuber, Patrick ; Hu, Yilin ; Ribbe, Markus W. ; Neese, Frank ; Bergmann, Uwe ; DeBeer, Serena</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c602t-e8afe27967b048e462824e88effe8e664aaed1c9d155c7aa8fc57e619cdf615d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Ammonia</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Artificial satellites</topic><topic>Atoms</topic><topic>Azotobacter vinelandii - chemistry</topic><topic>Biocatalysis</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Carbon</topic><topic>Carbon - chemistry</topic><topic>catalytic activity</topic><topic>Electrons</topic><topic>Emission spectroscopy</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Infrared spectroscopy</topic><topic>Iron</topic><topic>Ligands</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>Molybdoferredoxin - chemistry</topic><topic>Molybdoferredoxin - metabolism</topic><topic>Nitrogen</topic><topic>Nitrogen - chemistry</topic><topic>nitrogenase</topic><topic>Oxidation</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases</topic><topic>oxygen</topic><topic>Oxygen - chemistry</topic><topic>Proteins</topic><topic>Reduction</topic><topic>Spectrometry, X-Ray Emission</topic><topic>Spectroscopy</topic><topic>X ray spectroscopy</topic><topic>X-rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lancaster, Kyle M.</creatorcontrib><creatorcontrib>Roemelt, Michael</creatorcontrib><creatorcontrib>Ettenhuber, Patrick</creatorcontrib><creatorcontrib>Hu, Yilin</creatorcontrib><creatorcontrib>Ribbe, Markus W.</creatorcontrib><creatorcontrib>Neese, Frank</creatorcontrib><creatorcontrib>Bergmann, Uwe</creatorcontrib><creatorcontrib>DeBeer, Serena</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>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>MEDLINE - 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>Lancaster, Kyle M.</au><au>Roemelt, Michael</au><au>Ettenhuber, Patrick</au><au>Hu, Yilin</au><au>Ribbe, Markus W.</au><au>Neese, Frank</au><au>Bergmann, Uwe</au><au>DeBeer, Serena</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>X-ray Emission Spectroscopy Evidences a Central Carbon in the Nitrogenase Iron-Molybdenum Cofactor</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2011-11-18</date><risdate>2011</risdate><volume>334</volume><issue>6058</issue><spage>974</spage><epage>977</epage><pages>974-977</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>Nitrogenase is a complex enzyme that catalyzes the reduction of dinitrogen to ammonia. Despite insight from structural and biochemical studies, its structure and mechanism await full characterization. An iron-molybdenum cofactor (FeMoco) is thought to be the site of dinitrogen reduction, but the identity of a central atom in this cofactor remains unknown. Fe Kβ x-ray emission spectroscopy (XES) of intact nitrogenase MoFe protein, isolated FeMoco, and the FeMoco-deficient ΔnifB protein indicates that among the candidate atoms oxygen, nitrogen, and carbon, it is carbon that best fits the XES data. The experimental XES is supported by computational efforts, which show that oxidation and spin states do not affect the assignment of the central atom to C⁴⁺. Identification of the central atom will drive further studies on its role in catalysis.</abstract><cop>Washington, DC</cop><pub>American Association for the Advancement of Science</pub><pmid>22096198</pmid><doi>10.1126/science.1206445</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Ammonia Analytical, structural and metabolic biochemistry Artificial satellites Atoms Azotobacter vinelandii - chemistry Biocatalysis Biochemistry Biological and medical sciences Carbon Carbon - chemistry catalytic activity Electrons Emission spectroscopy Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Infrared spectroscopy Iron Ligands Models, Molecular Molecular Structure Molybdoferredoxin - chemistry Molybdoferredoxin - metabolism Nitrogen Nitrogen - chemistry nitrogenase Oxidation Oxidation-Reduction Oxidoreductases oxygen Oxygen - chemistry Proteins Reduction Spectrometry, X-Ray Emission Spectroscopy X ray spectroscopy X-rays |
| title | X-ray Emission Spectroscopy Evidences a Central Carbon in the Nitrogenase Iron-Molybdenum Cofactor |
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