{"@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/1363670319257202560.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1002/anie.201409928"}},{"identifier":{"@type":"URI","@value":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fanie.201409928"}},{"identifier":{"@type":"URI","@value":"https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.201409928"}}],"dc:title":[{"@value":"Highly Diastereoselective and Enantioselective Olefin Cyclopropanation Using Engineered Myoglobin‐Based Catalysts"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:title>Abstract</jats:title><jats:p>Using rational design, an engineered myoglobin‐based catalyst capable of catalyzing the cyclopropanation of aryl‐substituted olefins with catalytic proficiency (up to 46 800 turnovers) and excellent diastereo‐ and enantioselectivity (98–99.9 %) was developed. This transformation could be carried out in the presence of up to 20 g L<jats:sup>−1</jats:sup> olefin substrate with no loss in diastereo‐ and/or enantioselectivity. Mutagenesis and mechanistic studies support a cyclopropanation mechanism mediated by an electrophilic, heme‐bound carbene species and a model is provided to rationalize the stereopreference of the protein catalyst. This work shows that myoglobin constitutes a promising and robust scaffold for the development of biocatalysts with carbene‐transfer reactivity.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1383670319257202560","@type":"Researcher","foaf:name":[{"@value":"Melanie Bordeaux"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670319257202561","@type":"Researcher","foaf:name":[{"@value":"Vikas Tyagi"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670319257202562","@type":"Researcher","foaf:name":[{"@value":"Rudi Fasan"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"14337851"},{"@type":"EISSN","@value":"15213773"}],"prism:publicationName":[{"@value":"Angewandte Chemie International Edition"}],"dc:publisher":[{"@value":"Wiley"}],"prism:publicationDate":"2014-12-23","prism:volume":"54","prism:number":"6","prism:startingPage":"1744","prism:endingPage":"1748"},"reviewed":"false","dc:rights":["http://onlinelibrary.wiley.com/termsAndConditions#vor"],"url":[{"@id":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fanie.201409928"},{"@id":"https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.201409928"}],"createdAt":"2014-12-23","modifiedAt":"2023-10-16","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050019590267566464","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Redox Engineering of Myoglobin by Cofactor Substitution to Enhance Cyclopropanation Reactivity"}]},{"@id":"https://cir.nii.ac.jp/crid/1050581168899666944","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Chitin- and Streptavidin- Mediated Affinity Purification Systems: A Screening Platform for Enzyme Discovery"},{"@value":"Chitin‐ and Streptavidin‐Mediated Affinity Purification Systems: A Screening Platform for Enzyme Discovery"}]},{"@id":"https://cir.nii.ac.jp/crid/1050858784329394688","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Design of artificial metalloproteins/metalloenzymes by tuning noncovalent interactions"}]},{"@id":"https://cir.nii.ac.jp/crid/1360025429420275968","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Production of Phenyldiazene Derivatives Using the Biosynthetic Pathway of an Aromatic Diazo Group‐Containing Natural Product from an Actinomycete"}]},{"@id":"https://cir.nii.ac.jp/crid/1360298757195928192","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Engineering of hemoproteins"}]},{"@id":"https://cir.nii.ac.jp/crid/1360567182137272832","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Preparation and characterization of myoglobin reconstituted with Fe(II) oxaporphyrin: The monoanionic macrocycle provides unique cyanide binding behavior for the ferrous species"}]},{"@id":"https://cir.nii.ac.jp/crid/1360572092633557632","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Myoglobins engineered with artificial cofactors serve as artificial metalloenzymes and models of natural enzymes"}]},{"@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                    - 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