{"@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/1363388843782344192.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1038/ncomms8789"}},{"identifier":{"@type":"URI","@value":"https://www.nature.com/articles/ncomms8789.pdf"}},{"identifier":{"@type":"URI","@value":"https://www.nature.com/articles/ncomms8789"}}],"dc:title":[{"@value":"Engineering a dirhodium artificial metalloenzyme for selective olefin cyclopropanation"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:title>Abstract</jats:title><jats:p>Artificial metalloenzymes (ArMs) formed by incorporating synthetic metal catalysts into protein scaffolds have the potential to impart to chemical reactions selectivity that would be difficult to achieve using metal catalysts alone. In this work, we covalently link an alkyne-substituted dirhodium catalyst to a prolyl oligopeptidase containing a genetically encoded L-4-azidophenylalanine residue to create an ArM that catalyses olefin cyclopropanation. Scaffold mutagenesis is then used to improve the enantioselectivity of this reaction, and cyclopropanation of a range of styrenes and donor–acceptor carbene precursors were accepted. The ArM reduces the formation of byproducts, including those resulting from the reaction of dirhodium–carbene intermediates with water. This shows that an ArM can improve the substrate specificity of a catalyst and, for the first time, the water tolerance of a metal-catalysed reaction. Given the diversity of reactions catalysed by dirhodium complexes, we anticipate that dirhodium ArMs will provide many unique opportunities for selective catalysis.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1383388843782344321","@type":"Researcher","foaf:name":[{"@value":"Poonam Srivastava"}]},{"@id":"https://cir.nii.ac.jp/crid/1383388843782344192","@type":"Researcher","foaf:name":[{"@value":"Hao Yang"}]},{"@id":"https://cir.nii.ac.jp/crid/1383388843782344320","@type":"Researcher","foaf:name":[{"@value":"Ken Ellis-Guardiola"}]},{"@id":"https://cir.nii.ac.jp/crid/1383388843782344193","@type":"Researcher","foaf:name":[{"@value":"Jared C. Lewis"}]}],"publication":{"publicationIdentifier":[{"@type":"EISSN","@value":"20411723"}],"prism:publicationName":[{"@value":"Nature Communications"}],"dc:publisher":[{"@value":"Springer Science and Business Media LLC"}],"prism:publicationDate":"2015-07-24","prism:volume":"6","prism:number":"1","prism:startingPage":"7789"},"reviewed":"false","dc:rights":["https://creativecommons.org/licenses/by/4.0","https://creativecommons.org/licenses/by/4.0"],"url":[{"@id":"https://www.nature.com/articles/ncomms8789.pdf"},{"@id":"https://www.nature.com/articles/ncomms8789"}],"createdAt":"2015-07-24","modifiedAt":"2023-08-12","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360021390569735680","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Cross-Linked Crystals of Dirhodium Tetraacetate/RNase A Adduct Can Be Used as Heterogeneous Catalysts"}]},{"@id":"https://cir.nii.ac.jp/crid/1360290617849264256","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Incorporation of a Cp*Rh(III)-dithiophosphate Cofactor with Latent Activity into a Protein Scaffold Generates a Biohybrid Catalyst Promoting C(sp<sup>2</sup>)–H Bond Functionalization"}]},{"@id":"https://cir.nii.ac.jp/crid/1360298761974390272","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Prodrug Activation by Gold Artificial Metalloenzyme‐Catalyzed Synthesis of Phenanthridinium Derivatives via Hydroamination"}]},{"@id":"https://cir.nii.ac.jp/crid/1360565165972391808","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Construction of a hybrid biocatalyst containing a covalently-linked terpyridine metal complex within a cavity of aponitrobindin"}]},{"@id":"https://cir.nii.ac.jp/crid/1360568468305730944","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"An artificial metalloenzyme biosensor can detect ethylene gas in fruits and Arabidopsis leaves"}]},{"@id":"https://cir.nii.ac.jp/crid/1360572092711540736","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Artificial Metalloenzymes: From Selective Chemical Transformations to Biochemical Applications"}]},{"@id":"https://cir.nii.ac.jp/crid/1360572092786604928","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Enhanced\n                    <i>cis</i>\n                    - and enantioselective cyclopropanation of styrene catalysed by cytochrome P450BM3 using decoy molecules"}]},{"@id":"https://cir.nii.ac.jp/crid/1360572092825791488","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Construction of a whole-cell biohybrid catalyst using a Cp*Rh(III)-dithiophosphate complex as a precursor of a metal cofactor"}]},{"@id":"https://cir.nii.ac.jp/crid/1360846641590504064","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Catalytic Cyclopropanation by Myoglobin Reconstituted with Iron Porphycene: Acceleration of Catalysis due to Rapid Formation of the Carbene Species"}]},{"@id":"https://cir.nii.ac.jp/crid/1360848658048079104","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Hemoproteins Reconstituted with Artificial Metal Complexes as Biohybrid Catalysts"}]},{"@id":"https://cir.nii.ac.jp/crid/1360848658056231296","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Mixed Ligated Tris(amidinate)dimolybdenum Complexes as Catalysts for Radical Addition of CCl<sub>4</sub> to 1-Hexene: Leaving Ligand Lability Controls Catalyst Activity"}]},{"@id":"https://cir.nii.ac.jp/crid/1360869856022835584","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"A thiopyridine-bound mirror-image copper center in an artificial non-heme metalloenzyme"}]},{"@id":"https://cir.nii.ac.jp/crid/1361131644199943168","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Coordination-Induced Self-Assembly of a Heteroleptic Paddlewheel-Type Dirhodium Complex"}]},{"@id":"https://cir.nii.ac.jp/crid/1361975843220206976","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Biocompatibility and therapeutic potential of glycosylated albumin artificial metalloenzymes"}]},{"@id":"https://cir.nii.ac.jp/crid/1390002184880674176","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Unlocking the therapeutic potential of artificial metalloenzymes"}]},{"@id":"https://cir.nii.ac.jp/crid/2050870367081136768","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Exploring and adapting the molecular selectivity of artificial metalloenzymes"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1038/ncomms8789"},{"@type":"CROSSREF","@value":"10.1016/j.jinorgbio.2015.12.026_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.1021/acs.inorgchem.3c00852_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.1246/bcsj.20200316_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.1021/acs.inorgchem.0c02245_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.2183/pjab.96.007_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.1038/s41467-019-13758-2_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.1021/jacs.7b10154_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.1002/anie.202100369_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.3390/molecules25132989_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.1039/d0cc04883f_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.1016/j.jinorgbio.2020.111352_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.1038/s41929-019-0317-4_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.1021/acs.accounts.8b00676_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.1021/acs.inorgchem.6b02525_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.1016/j.jinorgbio.2024.112694_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"},{"@type":"CROSSREF","@value":"10.3390/cryst10020085_references_DOI_6jp6Fb9EMgevKwFLV6HHZlCDoGV"}]}