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dc.contributor.authorSenge, Mathias
dc.contributor.authorNorvaiša, Karolis
dc.contributor.authorFlanagan, Keith J.
dc.contributor.authorGibbons, Dáire
dc.date.accessioned2020-01-10T16:02:06Z
dc.date.available2020-01-10T16:02:06Z
dc.date.issued2019
dc.date.submitted2019en
dc.identifier.citationNorvaiša, K., Flanagan, K.J., Gibbons, D. & Senge, M.O., Conformational Re-engineering of Porphyrins as Receptors with Switchable NH???X-Type Binding Modes, Angewandte Chemie International Edition, 58, 2019, 16553-16557en
dc.identifier.otherY
dc.identifier.urihttps://onlinelibrary.wiley.com/doi/full/10.1002/anie.201907929
dc.identifier.urihttp://hdl.handle.net/2262/91291
dc.descriptionPUBLISHEDen
dc.description.abstractThe selectivity and functional variability of porphyrin cofactors are typically based on substrate binding of metalloporphyrins wherein the pyrrole nitrogen units only serve to chelate the metal ions. Yet, using the porphyrin inner core system for other functions is possible through conformational engineering. As a first step towards porphyrin “enzyme‐like” active centers, a structural and spectroscopic study of substrate binding to the inner core porphyrin system shows that a highly saddle‐distorted porphyrin with peripheral amino receptor groups (1, 2,3,7,8,12,13,17,18‐octaethyl‐5,10,15,20‐tetrakis(2‐aminophenyl)porphyrin) coordinates analytes in a switchable manner dependent on the acidity of the solution. The supramolecular ensemble exhibits exceptionally high affinity to and selectivity for the pyrophosphate anion (2.26±0.021)×109 m−1. 1H NMR spectroscopic studies provided insight into the likely mode of binding and the characterization of atropisomers, all four of which were also studied by X‐ray crystallography.en
dc.format.extent16553-16557en
dc.language.isoenen
dc.relation.ispartofseriesAngewandte Chemie International Edition;
dc.relation.ispartofseries58;
dc.rightsYen
dc.subjectConformational designen
dc.subjectNonplanar porphyrinsen
dc.subjectPorphyrinoidsen
dc.subjectPyrophosphateen
dc.subjectSensorsen
dc.titleConformational Re-engineering of Porphyrins as Receptors with Switchable NH???X-Type Binding Modesen
dc.typeJournal Articleen
dc.type.supercollectionscholarly_publicationsen
dc.type.supercollectionrefereed_publicationsen
dc.identifier.peoplefinderurlhttp://people.tcd.ie/sengem
dc.identifier.rssinternalid209797
dc.rights.ecaccessrightsopenAccess
dc.subject.TCDThemeNanoscience & Materialsen
dc.subject.TCDThemeNext Generation Medical Devicesen
dc.subject.TCDTagPORPHYRINen
dc.subject.TCDTagPorphyrin Chemistryen
dc.status.accessibleNen


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