2019
DOI: 10.1016/bs.mie.2019.03.013
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EPR spectroscopy on flavin radicals in flavoproteins

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Cited by 14 publications
(35 citation statements)
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“…Additionally, long range electrostatic and van der Waals interactions are critical in determining the flavin's overall properties. Protein‐bound flavin thus experiences a highly constrained, interactive, and perturbing environment, which is able to bring about a wide range of reactivities, favor different redox and protonation states, 48 and produce different spin configurations 49–51 . Thus, explicit treatment of the immediate environment (amino acid side‐chains and solvent molecules) is essential for an accurate description of structural or electronic properties of flavin cofactors.…”
Section: Models Of Flavin‐based Systemsmentioning
confidence: 99%
“…Additionally, long range electrostatic and van der Waals interactions are critical in determining the flavin's overall properties. Protein‐bound flavin thus experiences a highly constrained, interactive, and perturbing environment, which is able to bring about a wide range of reactivities, favor different redox and protonation states, 48 and produce different spin configurations 49–51 . Thus, explicit treatment of the immediate environment (amino acid side‐chains and solvent molecules) is essential for an accurate description of structural or electronic properties of flavin cofactors.…”
Section: Models Of Flavin‐based Systemsmentioning
confidence: 99%
“…Previous investigations showed that Fre catalyzes the reduction of flavins by NAD(P)H by positioning in its active site these two substrates in such a way to favor the hydride transfer from the C-4 atom position of the NADH nicotinamide moiety to the N-5 atom of the flavin isoalloxazine ring. 34,37,40 The STEAP structures show that the flavin cofactor is located rather on the surface of the cytosolic side of the transmembrane domain. 41 One can hypothesis that during the reduction by Fre, the FMN cofactor moves from its MsrQ binding site toward the Fre substrates cavity (Figure 9A).…”
Section: Electronic Paramagnetic Resonance On Msrqmentioning
confidence: 99%
“…W-band Mims-ENDOR of the [7α,9-2 H4]LOV* sample, recorded at 120 K and 20 K, afforded tensors of remarkably different shapes (see Figures 4 and 5). We assume a comparable behavior of the protons (deuterons) attached to C(8α) and C(7α) if samples are cooled down from 120 K to 20 K. In our model, the deuterated methyl group attached to C (7) does not rotate at 20 K within the time scale of the Mims-ENDOR experiment, which is reflected by three individual hf tensors of rhombic symmetry. On the other hand, methyl group rotation is fast at 120 K, and consequently, the three deuterons become magnetically equivalent and merge to one single hf tensor of axial symmetry.…”
Section: Temperature Dependence Of the 7α Methyl Group Rotationmentioning
confidence: 99%
“…This work was recently repeated with an engineered LOV photoreceptor YF1 and with flavodoxin, both investigated proteins showed similar behavior. [34][35] With the present contribution, we expand our knowledge on this phenomenon by investigating the 7α methyl group attached to C (7). We were particularly interested in answering the question, whether the 7α methyl group exhibits a similar response to a temperature variation as does the adjacent 8α-methyl group.…”
Section: Introductionmentioning
confidence: 99%
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