Controlling the optical and catalytic properties of artificial metalloenzyme photocatalysts using chemogenetic engineering

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dc.contributor.authorZubi, Yasmine S.en
dc.contributor.authorLiu, Bingqingen
dc.contributor.authorGu, Yifanen
dc.contributor.authorSahoo, Dipankaren
dc.contributor.authorLewis, Jared C.en
dc.date.accessioned2022-08-22T13:47:28Zen
dc.date.available2022-08-22T13:47:28Zen
dc.date.issued2022-02-02en
dc.description.abstractVisible light photocatalysis enables a broad range of organic transformations that proceed via single electron or energy transfer. Metal polypyridyl complexes are among the most commonly employed visible light photocatalysts. The photophysical properties of these complexes have been extensively studied and can be tuned by modifying the substituents on the pyridine ligands. On the other hand, ligand modifications that enable substrate binding to control reaction selectivity remain rare. Given the exquisite control that enzymes exert over electron and energy transfer processes in nature, we envisioned that artificial metalloenzymes (ArMs) created by incorporating Ru(ii) polypyridyl complexes into a suitable protein scaffold could provide a means to control photocatalyst properties. This study describes approaches to create covalent and non-covalent ArMs from a variety of Ru(ii) polypyridyl cofactors and a prolyl oligopeptidase scaffold. A panel of ArMs with enhanced photophysical properties were engineered, and the nature of the scaffold/cofactor interactions in these systems was investigated. These ArMs provided higher yields and rates than Ru(Bpy)(3)(2+) for the reductive cyclization of dienones and the [2 + 2] photocycloaddition between C-cinnamoyl imidazole and 4-methoxystyrene, suggesting that protein scaffolds could provide a means to improve the efficiency of visible light photocatalysts.en
dc.description.notesThis study was supported by the U.S. Army Research Laboratory and the U.S. Army Research Office under Contract/Grant W911NF-19-1-0074 and by an NSF CAREER Award to J. C. L. (CHE-1351991). Y. S. Z. gratefully acknowledges receipt of a predoctoral fellowship from the Graduate Training Program in Quantitative and Chemical Biology at Indiana University (T32 GM131994). NMR data were acquired on a spectrometer funded by the NSF (MRI CHE-1920026) using a Prodigy probe that was partially funded by the Indiana Clinical and Translational Sciences Institute. We thank Dr Jonathan Trinidad for assistance with intact protein ESI-MS; Dr Giovanni GonzalezGutierrez for assistance with various instrumentation in the IU Physical Biochemistry Instrumentation Facility and for allowing us to borrow a low-volume cuvette for luminescence measurements; and Prof. Amar Flood for access to a UV-Vis spectrophotometer and a.uorometer. We thank IU Mechanical Instrument Services and IU Electronic Instrument Services, including Mr John Poehlman and Ms Rose Burch.eld in particular, for assistance with the design and fabrication of the photoreactor used in these studies.en
dc.description.sponsorshipU.S. Army Research Laboratory [W911NF-19-1-0074]; U.S. Army Research Office [W911NF-19-1-0074]; NSF CAREER Award [CHE-1351991]; Graduate Training Program in Quantitative and Chemical Biology at Indiana University [T32 GM131994]; NSF - Indiana Clinical and Translational Sciences Institute [MRI CHE-1920026]en
dc.description.versionPublished versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.1039/d1sc05792hen
dc.identifier.eissn2041-6539en
dc.identifier.issn2041-6520en
dc.identifier.issue5en
dc.identifier.pmid35222930en
dc.identifier.urihttp://hdl.handle.net/10919/111574en
dc.identifier.volume13en
dc.language.isoenen
dc.publisherRoyal Society of Chemistryen
dc.rightsCreative Commons Attribution-NonCommercial 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/en
dc.subjectcoupled electron-transferen
dc.subjectphotoredox catalysisen
dc.subjectcomplexesen
dc.subjectruthenium(ii)en
dc.subjectbindingen
dc.subjectplastocyaninen
dc.subjectmetalloproteinsen
dc.subjectphotochemistryen
dc.subjectstreptavidinen
dc.subjectcoordinationen
dc.titleControlling the optical and catalytic properties of artificial metalloenzyme photocatalysts using chemogenetic engineeringen
dc.title.serialChemical Scienceen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten

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