Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor
The identity of the interstitial light atom in the center of the FeMo cofactor of nitrogenase has been enigmatic since its discovery. Atomic-resolution x-ray diffraction data and an electron spin echo envelope modulation (ESEEM) analysis now provide direct evidence that the ligand is a carbon specie...
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Veröffentlicht in: | Science (American Association for the Advancement of Science) 2011-11, Vol.334 (6058), p.940-940 |
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creator | Spatzal, Thomas Aksoyoglu, Müge Zhang, Limei Andrade, Susana L. A. Schleicher, Erik Weber, Stefan Rees, Douglas C. Einsle, Oliver |
description | The identity of the interstitial light atom in the center of the FeMo cofactor of nitrogenase has been enigmatic since its discovery. Atomic-resolution x-ray diffraction data and an electron spin echo envelope modulation (ESEEM) analysis now provide direct evidence that the ligand is a carbon species. |
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A. ; Schleicher, Erik ; Weber, Stefan ; Rees, Douglas C. ; Einsle, Oliver</creator><creatorcontrib>Spatzal, Thomas ; Aksoyoglu, Müge ; Zhang, Limei ; Andrade, Susana L. A. ; Schleicher, Erik ; Weber, Stefan ; Rees, Douglas C. ; Einsle, Oliver</creatorcontrib><description>The identity of the interstitial light atom in the center of the FeMo cofactor of nitrogenase has been enigmatic since its discovery. Atomic-resolution x-ray diffraction data and an electron spin echo envelope modulation (ESEEM) analysis now provide direct evidence that the ligand is a carbon species.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1214025</identifier><identifier>PMID: 22096190</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Association for the Advancement of Science</publisher><subject>Atoms ; Azotobacter vinelandii - chemistry ; Biological and medical sciences ; BREVIA ; Carbon ; Carbon - chemistry ; Catalysis ; Crystalline structure ; Crystallography, X-Ray ; Electron Spin Resonance Spectroscopy ; Evidence ; Fundamental and applied biological sciences. 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A.</creatorcontrib><creatorcontrib>Schleicher, Erik</creatorcontrib><creatorcontrib>Weber, Stefan</creatorcontrib><creatorcontrib>Rees, Douglas C.</creatorcontrib><creatorcontrib>Einsle, Oliver</creatorcontrib><title>Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>The identity of the interstitial light atom in the center of the FeMo cofactor of nitrogenase has been enigmatic since its discovery. Atomic-resolution x-ray diffraction data and an electron spin echo envelope modulation (ESEEM) analysis now provide direct evidence that the ligand is a carbon species.</description><subject>Atoms</subject><subject>Azotobacter vinelandii - chemistry</subject><subject>Biological and medical sciences</subject><subject>BREVIA</subject><subject>Carbon</subject><subject>Carbon - chemistry</subject><subject>Catalysis</subject><subject>Crystalline structure</subject><subject>Crystallography, X-Ray</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Evidence</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Isotopic labeling</subject><subject>ligands</subject><subject>Models, Molecular</subject><subject>Molecular biophysics</subject><subject>Molecular Structure</subject><subject>Molybdoferredoxin - chemistry</subject><subject>Nitrogen</subject><subject>Nitrogen - chemistry</subject><subject>nitrogenase</subject><subject>Structure in molecular biology</subject><subject>X-ray diffraction</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>eNp9kT1vFDEYhC1ERC4HNRVohRRBs4lff7sACZ0SEimBBmrL6_MGn_bsYO9F4t_j1S3HR5HKxTzvaDyD0EvAZwBEnBcXfHT-DAgwTPgTtACseasJpk_RAmMqWoUlP0YnpWwwrpqmz9AxIVgL0HiB3l88hPVk0fQpN9dx9LmMYQx2aFY2dyk2ITafw5jTnY-2-ObS36ZmlXrrxpSfo6PeDsW_mN8l-nZ58XV11d58-XS9-njTOi7x2DIBHHTnKFddR7UEzRz1QkqvnGeCWdJXXVOwkq1rQoIVKM6VEr3UTnG6RB_2vve7buvXzscx28Hc57C1-adJNph_lRi-m7v0YCgRigpZDd7OBjn92Pkymm0ozg-DjT7titGYCwmUQiXfPUqS2iJleoKX6M1_6CbtcqxFVD_GCQc8RT_fQy6nUrLvD6kBm2lDM29o5g3rxeu_P3vgf49WgdMZsMXZoc82ulD-cKy2B3QyerXnNqVuddBZ1UBSQX8B-zus3Q</recordid><startdate>20111118</startdate><enddate>20111118</enddate><creator>Spatzal, Thomas</creator><creator>Aksoyoglu, Müge</creator><creator>Zhang, Limei</creator><creator>Andrade, Susana L. 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Psychology</topic><topic>Isotopic labeling</topic><topic>ligands</topic><topic>Models, Molecular</topic><topic>Molecular biophysics</topic><topic>Molecular Structure</topic><topic>Molybdoferredoxin - chemistry</topic><topic>Nitrogen</topic><topic>Nitrogen - chemistry</topic><topic>nitrogenase</topic><topic>Structure in molecular biology</topic><topic>X-ray diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Spatzal, Thomas</creatorcontrib><creatorcontrib>Aksoyoglu, Müge</creatorcontrib><creatorcontrib>Zhang, Limei</creatorcontrib><creatorcontrib>Andrade, Susana L. 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subjects | Atoms Azotobacter vinelandii - chemistry Biological and medical sciences BREVIA Carbon Carbon - chemistry Catalysis Crystalline structure Crystallography, X-Ray Electron Spin Resonance Spectroscopy Evidence Fundamental and applied biological sciences. Psychology Isotopic labeling ligands Models, Molecular Molecular biophysics Molecular Structure Molybdoferredoxin - chemistry Nitrogen Nitrogen - chemistry nitrogenase Structure in molecular biology X-ray diffraction |
title | Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor |
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