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dc.contributor.authorLowe, Phillip T.
dc.contributor.authorCobb, Steven L.
dc.contributor.authorO'Hagan, David
dc.date.accessioned2020-07-24T23:36:06Z
dc.date.available2020-07-24T23:36:06Z
dc.date.issued2019-08-28
dc.identifier260859368
dc.identifierbc325925-d178-42c1-8535-efe9679f7c61
dc.identifier85070705601
dc.identifier000481416200008
dc.identifier.citationLowe , P T , Cobb , S L & O'Hagan , D 2019 , ' An enzymatic Finkelstein reaction : fluorinase catalyses direct halogen exchange ' , Organic & Biomolecular Chemistry , vol. 17 , no. 32 , pp. 7493-7496 . https://doi.org/10.1039/C9OB01625Ben
dc.identifier.issn1477-0520
dc.identifier.otherBibtex: urn:f31175a170f124ab5f3933a18eca40d9
dc.identifier.otherORCID: /0000-0002-0510-5552/work/68281291
dc.identifier.otherORCID: /0000-0003-1568-0750/work/122719953
dc.identifier.urihttps://hdl.handle.net/10023/20336
dc.descriptionWe thank the Engineering and Physical Sciences Research Council, UK, for a research grant.en
dc.description.abstractThe fluorinase enzyme from Streptomyces cattleya is shown to catalyse a direct displacement of bromide and iodide by fluoride ion from 5′-bromodeoxyadenosine (5′-BrDA) and 5′-iododeoxyadenosine (5′-IDA) respectively to form 5′-fluorodeoxyadenosine (5′-FDA) in the absence of L-methionine (L-Met) or S-adenosyl-L-methionine (SAM). 5′-BrDA is the most efficient substrate for this enzyme catalysed Finkelstein reaction.
dc.format.extent4
dc.format.extent626327
dc.language.isoeng
dc.relation.ispartofOrganic & Biomolecular Chemistryen
dc.subjectQD Chemistryen
dc.subjectNDASen
dc.subject.lccQDen
dc.titleAn enzymatic Finkelstein reaction : fluorinase catalyses direct halogen exchangeen
dc.typeJournal articleen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.identifier.doihttps://doi.org/10.1039/C9OB01625B
dc.description.statusPeer revieweden
dc.date.embargoedUntil2020-07-25


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