Matches in SemOpenAlex for { <https://semopenalex.org/work/W3201121350> ?p ?o ?g. }
- W3201121350 abstract "Abstract Flavocoenzymes are nearly ubiquitous cofactors that are involved in the catalysis and regulation of a wide range of biological processes including some light-induced ones, such as the photolyase-mediated DNA repair, magnetoreception of migratory birds, and the blue-light driven phototropism in plants. One of the factors that enable versatile flavin-coenzyme biochemistry and biophysics is the fine-tuning of the cofactor’s frontier orbital by interactions with the protein environment. Probing the singly-occupied molecular orbital (SOMO) of the intermediate radical state of flavins is therefore a prerequisite for a thorough understanding of the diverse functions of the flavoprotein family. This may be ultimately achieved by unravelling the hyperfine structure of a flavin by electron paramagnetic resonance. In this contribution we present a rigorous approach to obtaining a hyperfine map of the flavin’s chromophoric 7,8-dimethyl isoalloxazine unit at an as yet unprecedented level of resolution and accuracy. We combine powerful high-microwave-frequency/high-magnetic-field electron–nuclear double resonance (ENDOR) with 13 C isotopologue editing as well as spectral simulations and density functional theory calculations to measure and analyse 13 C hyperfine couplings of the flavin cofactor in DNA photolyase. Our data will provide the basis for electronic structure considerations for a number of flavin radical intermediates occurring in blue-light photoreceptor proteins." @default.
- W3201121350 created "2021-09-27" @default.
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- W3201121350 date "2021-09-14" @default.
- W3201121350 modified "2023-10-14" @default.
- W3201121350 title "Selective 13C labelling reveals the electronic structure of flavocoenzyme radicals" @default.
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- W3201121350 doi "https://doi.org/10.1038/s41598-021-97588-7" @default.
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