{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1361137045228240384.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1126/science.aar2765"}},{"identifier":{"@type":"URI","@value":"https://syndication.highwire.org/content/doi/10.1126/science.aar2765"}},{"identifier":{"@type":"URI","@value":"https://www.science.org/doi/pdf/10.1126/science.aar2765"}}],"dc:title":[{"@value":"A bound reaction intermediate sheds light on the mechanism of nitrogenase"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:title>Sulfur steps aside for nitrogen</jats:title>\n                  <jats:p>\n                    Enzymatic conversion of molecular nitrogen to ammonia requires a dance of electrons and protons. The stage for that dance is the nitrogenase cofactor, a carefully constructed cluster of iron, sulfur, and carbon with homocitrate and, in some cases, bicarbonate appendages, as well as a secondary metal ion that defines the class of enzyme. The question of how this cofactor binds nitrogen has been vexingly difficult to answer. Sippel\n                    <jats:italic>et al.</jats:italic>\n                    report a high-resolution structure of the vanadium nitrogenase with a light atom, interpreted as nitrogen, bound to the FeV cofactor. A sulfur atom is displaced from the cofactor in this structure and is observed resting in a holding site formed by rearrangement of a glutamine residue. The putative bridging nitrogen atom suggests that diatomic nitrogen may bind to the cluster in a head-on manner, with the glutamine side chain stabilizing protonated intermediates as they are reduced.\n                  </jats:p>\n                  <jats:p>\n                    <jats:italic>Science</jats:italic>\n                    , this issue p.\n                    <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" issue=\"6383\" page=\"1484\" related-article-type=\"in-this-issue\" vol=\"359\" xlink:href=\"10.1126/science.aar2765\">1484</jats:related-article>\n                  </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1381137045228240390","@type":"Researcher","foaf:name":[{"@value":"Daniel Sippel"}],"jpcoar:affiliationName":[{"@value":"Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstraße 21, 79104 Freiburg, Germany."}]},{"@id":"https://cir.nii.ac.jp/crid/1381137045228240386","@type":"Researcher","foaf:name":[{"@value":"Michael Rohde"}],"jpcoar:affiliationName":[{"@value":"Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstraße 21, 79104 Freiburg, Germany."}]},{"@id":"https://cir.nii.ac.jp/crid/1381137045228240387","@type":"Researcher","foaf:name":[{"@value":"Julia Netzer"}],"jpcoar:affiliationName":[{"@value":"Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstraße 21, 79104 Freiburg, Germany."}]},{"@id":"https://cir.nii.ac.jp/crid/1381137045228240388","@type":"Researcher","foaf:name":[{"@value":"Christian Trncik"}],"jpcoar:affiliationName":[{"@value":"Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstraße 21, 79104 Freiburg, Germany."}]},{"@id":"https://cir.nii.ac.jp/crid/1381137045228240385","@type":"Researcher","foaf:name":[{"@value":"Jakob Gies"}],"jpcoar:affiliationName":[{"@value":"Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstraße 21, 79104 Freiburg, Germany."}]},{"@id":"https://cir.nii.ac.jp/crid/1381137045228240393","@type":"Researcher","foaf:name":[{"@value":"Katharina Grunau"}],"jpcoar:affiliationName":[{"@value":"Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstraße 21, 79104 Freiburg, Germany."}]},{"@id":"https://cir.nii.ac.jp/crid/1381137045228240384","@type":"Researcher","foaf:name":[{"@value":"Ivana Djurdjevic"}],"jpcoar:affiliationName":[{"@value":"Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstraße 21, 79104 Freiburg, Germany."}]},{"@id":"https://cir.nii.ac.jp/crid/1381137045228240392","@type":"Researcher","foaf:name":[{"@value":"Laure Decamps"}],"jpcoar:affiliationName":[{"@value":"Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstraße 21, 79104 Freiburg, Germany."}]},{"@id":"https://cir.nii.ac.jp/crid/1381137045228240389","@type":"Researcher","foaf:name":[{"@value":"Susana L. A. Andrade"}],"jpcoar:affiliationName":[{"@value":"Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstraße 21, 79104 Freiburg, Germany."},{"@value":"BIOSS Centre for Biological Signalling Studies, Schänzlestraße 1, 79104 Freiburg, Germany."}]},{"@id":"https://cir.nii.ac.jp/crid/1381137045228240391","@type":"Researcher","foaf:name":[{"@value":"Oliver Einsle"}],"jpcoar:affiliationName":[{"@value":"Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstraße 21, 79104 Freiburg, Germany."},{"@value":"BIOSS Centre for Biological Signalling Studies, Schänzlestraße 1, 79104 Freiburg, Germany."},{"@value":"Freiburg Institute for Advanced Studies, 79104 Freiburg, Germany."}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00368075"},{"@type":"EISSN","@value":"10959203"}],"prism:publicationName":[{"@value":"Science"}],"dc:publisher":[{"@value":"American Association for the Advancement of Science (AAAS)"}],"prism:publicationDate":"2018-03-30","prism:volume":"359","prism:number":"6383","prism:startingPage":"1484","prism:endingPage":"1489"},"reviewed":"false","url":[{"@id":"https://syndication.highwire.org/content/doi/10.1126/science.aar2765"},{"@id":"https://www.science.org/doi/pdf/10.1126/science.aar2765"}],"createdAt":"2018-03-29","modifiedAt":"2024-01-15","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050004953482645760","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Metal–Sulfur Compounds in N2 Reduction and Nitrogenase-Related Chemistry"},{"@value":"Metal–Sulfur Compounds in N<sub>2</sub> Reduction and Nitrogenase-Related Chemistry"}]},{"@id":"https://cir.nii.ac.jp/crid/1050013244133092480","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Nitrogen reduction by the Fe sites of synthetic [Mo₃S₄Fe] cubes"}]},{"@id":"https://cir.nii.ac.jp/crid/1360016870444628096","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Activation of unsaturated small molecules by bio-relevant multinuclear metal-sulfur clusters"}]},{"@id":"https://cir.nii.ac.jp/crid/1360016870541076096","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Incorporation of an Asymmetric Mo−Fe−S Cluster as an Artificial Cofactor into Nitrogenase"}]},{"@id":"https://cir.nii.ac.jp/crid/1360017282232737280","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Transition metal catalyzed cross-coupling and nitrogen reduction reactions: Lessons from computational studies"}]},{"@id":"https://cir.nii.ac.jp/crid/1360290617807499136","@type":"Article","resourceType":"学術雑誌論文(journal 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