A neutron diffraction investigation of high valent doped barium ferrite with wideband tunable microwave absorption

The barium ferrite BaTixFe12−xO19 (x = 0.2, 0.4, 0.6, 0.8) (BFTO-x) ceramics doped by Ti4+ were synthesized by a modified sol—gel method. The crystal structure and magnetic structure of the samples were determined by neutron diffraction, and confirm that the BFTO-x ceramics were high quality single phase with sheet microstructure. With x increasing from 0.2 to 0.8, the saturation magnetization (Ms) decreases gradually but the change trend of coercivity (Hc) is complex under the synergy of the changed grain size and the magnetic crystal anisotropy field. Relying on the high valence of Ti4+, double resonance peaks are obtained in the curves of the imaginary part of magnetic conductivity (μ″) and the resonance peaks could move toward the low frequency with the increase of x, which facilitate the samples perform an excellent wideband modulation microwave absorption property. In the x = 0.2 sample, the maximum reflection loss (RL) can reach −44.9 dB at the thickness of only 1.8 mm, and the bandwidth could reach 5.28 GHz at 2 mm when RL is less than −10 dB. All the BFTO-x ceramics show excellent frequency modulation ability varying from 18 (x = 0.8) to 4 GHz (x = 0.4), which covers 81% of the investigated frequency in microwave absorption field. This work not only implements the tunable of electromagnetic parameters but also broadens the application of high-performance microwave absorption devices.

In situ distance measurements in a membrane transporter using maleimide functionalized orthogonal spin labels and 5-pulse electron double resonance spectroscopy

Spectroscopic investigation of membrane proteins in their native environment is a challenging task. Earlier we demonstrated the feasibility to measure precise distances within outer membrane proteins in E. coli and native membranes using methanethiosulfonate (MTS) functionalized labels combined with pulsed electron double resonance spectroscopy. Here we show the application of maleimide functionalized Gd(III), nitroxide, and trityl labels for in situ distance measurement using the cobalamin transporter BtuB. These labels enabled distance measurements for BtuB in E. coli and native outer membranes and in the membranes maleimide-Gd-DOTA also is effective. Further, we show that the observable dipolar evolution time can be significantly prolonged in the native environments using the Carr-Purcell 5-pulse electron double resonance sequence. For a nitroxide-nitroxide pair, application of sech/tanh inversion pulses substantially suppressed the 4-pulse artifact at the Q- band frequency. In the case of a nitroxide-trityl pair, Gaussian pump pulses of varying amplitude are sufficient to suppress the artifact to the typical noise level. The feasibility of a range of bioresistant spin labels and the 5-pulse electron double resonance offers promising tools for investigating heterooligomeric membrane protein complexes in their native environment.

Photonic crystal meso-cavity with double resonance for second-harmonic generation

In this work, we study a composite zinc oxide photonic crystal that includes a meso-cavity coupled to a photonic crystal L3 microcavity to obtain a double resonance effect and second-harmonic generation conversion efficiency as high as 468 W-1. This exceptional conversion efficiency was attributed to the high quality-factors Q found in the fundamental and second-harmonic modes whose values were of the order of 105 and 106, respectively. Since the L3 microcavity plays a relevant role in the second-harmonic generation of the composite photonic crystal, we performed a calculation of its photonic band structure to observe the induced modes in its bandgap. Furthermore, we also found that the resonant mode adjusted to the frequency of the second-harmonic exhibits high Purcell factors of the order of 105. Hence, in a semiconductor material, it can be easily enhanced the light emission at the second harmonic frequency using an adequate driving fundamental frequency light beam. These results can stimulate the engineering of photonic nanostructures in semiconductor materials to achieve highly efficient non-linear effects with applications in cavity Quantum Electrodynamics.

Solution Tetrahydrobiopterin Radical vs. the Enzyme-Bound Radical: A Paramagnetic Reconciliation

Background: Nitric oxide synthase (NOS) catalyzes the formation of nitric oxide (NO) and citrulline from L-arginine, dioxygen (O2), and nicotinamide adenine dinucleotide phosphate (NADPH) in a two-step reaction, with the enzyme-bound intermediate Nω-hydroxy-L-arginine (NHA). Previous electron paramagnetic resonance (EPR) studies of NOS reaction have shown that (6R, 1'R, 2'S)-6-(l',2'-dihydroxypropyl)-5,6,7,8-tetrahydropterin (H4B) acts as a single electron donor in both steps of the reaction, resulting in the transient generation of a tetrahydropterin cation radical (H4B•+). Results: H4B•+ can also be chemically generated in strongly acidic solutions. EPR studies of chemically generated H4B•+ and similar pterin radicals date back to the 1960s. However, the reported paramagnetic parameters of H4B•+ in NOS do not seem to match the corresponding reported parameters for either H4B•+ or other pterin centered radicals chemically generated in solution. In particular, the rather isotropic hyperfine coupling of ca. 45 MHz for 1H6 of H4B•+ in NOS is at least 15 MHz larger than that of H4B•+ or any other previously studies pterin solution radical. In the work reported here, a combination of 9.5 - 9.8 GHz contentious wave (cw-) EPR, 34GHz 1H electron nuclear double resonance (ENDOR), spectral simulation and Density Functional Theory (DFT) calculations were used to investigate this seeming discrepancy. Conclusion: We demonstrated that the differences in the paramagnetic parameters of the chemically generated H4B radicals in solutions and those of the H4B radicals in NOS are consistent with the presence of two different conformers of the same cation radical in the two media.

Determination of Histidine Protonation States in Proteins by Fast Magic Angle Spinning NMR

Histidine residues play important structural and functional roles in proteins, such as serving as metal-binding ligands, mediating enzyme catalysis, and modulating proton channel activity. Many of these activities are modulated by the ionization state of the imidazole ring. Here we present a fast MAS NMR approach for the determination of protonation and tautomeric states of His at frequencies of 40–62 kHz. The experiments combine 1H detection with selective magnetization inversion techniques and transferred echo double resonance (TEDOR)–based filters, in 2D heteronuclear correlation experiments. We illustrate this approach using microcrystalline assemblies of HIV-1 CACTD-SP1 protein.

Selective 13C labelling reveals the electronic structure of flavocoenzyme radicals

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 13C isotopologue editing as well as spectral simulations and density functional theory calculations to measure and analyse 13C 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.