Magnetic fluctuations and superconductivity in Fe pnictides probed by electron spin resonance

The electron spin resonance absorption spectrum of Eu^{2+} ions serves as a probe of the normal and superconducting state in Eu_{0.5}K_{0.5}Fe_2As_2. The spin-lattice relaxation rate 1/T_1^{\rm ESR} obtained from the ESR linewidth exhibits a Korringa-like linear increase with temperature above T_C evidencing a normal Fermi-liquid behavior. Below 45 K deviations from the Korringa-law occur which are ascribed to enhanced magnetic fluctuations within the FeAs layers upon approaching the superconducting transition. Below T_C the spin-lattice relaxation rate 1/T_1^{\rm ESR} follows a T^{1.5}-behavior without the appearance of a coherence peak.Comment: 5 pages, 5 figure

Characterization of Hydrogen Plasma Defined Graphene Edges

We investigate the quality of hydrogen plasma defined graphene edges by Raman spectroscopy, atomic resolution AFM and low temperature electronic transport measurements. The exposure of graphite samples to a remote hydrogen plasma leads to the formation of hexagonal shaped etch pits, reflecting the anisotropy of the etch. Atomic resolution AFM reveals that the sides of these hexagons are oriented along the zigzag direction of the graphite crystal lattice and the absence of the D-peak in the Raman spectrum indicates that the edges are high quality zigzag edges. In a second step of the experiment, we investigate hexagon edges created in single layer graphene on hexagonal boron nitride and find a substantial D-peak intensity. Polarization dependent Raman measurements reveal that hydrogen plasma defined edges consist of a mixture of zigzag and armchair segments. Furthermore, electronic transport measurements were performed on hydrogen plasma defined graphene nanoribbons which indicate a high quality of the bulk but a relatively low edge quality, in agreement with the Raman data. These findings are supported by tight-binding transport simulations. Hence, further optimization of the hydrogen plasma etching technique is required to obtain pure crystalline graphene edges.Comment: 10 pages, 7 figure

Electron spin resonance in Eu based Fe pnictides

The phase diagrams of EuFe$_{2-x}$Co$_x$As$_2$ $(0 \leq x \leq 0.4)$ and EuFe$_2$As$_{2-y}$P$_y$ $(0 \leq y \leq 0.43)$ are investigated by Eu$^{2+}$ electron spin resonance (ESR) in single crystals. From the temperature dependence of the linewidth $\Delta H(T)$ of the exchange narrowed ESR line the spin-density wave (SDW) $(T < T_{\rm SDW})$ and the normal metallic regime $(T > T_{\rm SDW})$ are clearly distinguished. At $T > T_{\rm SDW}$ the isotropic linear increase of the linewidth is driven by the Korringa relaxation which measures the conduction-electron density of states at the Fermi level. For $T < T_{\rm SDW}$ the anisotropy probes the local ligand field, while the coupling to the conduction electrons disappears. With increasing substitution $x$ or $y$ the transition temperature $T_{\rm SDW}$ decreases linearly accompanied by a linear decrease of the Korringa-relaxation rate from 8 Oe/K at $x=y=0$ down to 3 Oe/K at the onset of superconductivity at $x \approx 0.2$ or at $y \approx 0.3$, above which it remains nearly constant. Comparative ESR measurements on single crystals of the Eu diluted SDW compound Eu$_{0.2}$Sr$_{0.8}$Fe$_2$As$_2$ and superconducting (SC) Eu$_{0.22}$Sr$_{0.78}$Fe$_{1.72}$Co$_{0.28}$As$_2$ corroborate the leading influence of the ligand field on the Eu$^{2+}$ spin relaxation in the SDW regime as well as the Korringa relaxation in the normal metallic regime. Like in Eu$_{0.5}$K$_{0.5}$Fe$_2$As$_2$ a coherence peak is not detected in the latter compound at $T_{\rm c}=21$ K, which is in agreement with the expected complex anisotropic SC gap structure

The role of a disulfide bridge in the stability and folding kinetics of Arabidopsis thaliana cytochrome c6A

Cytochrome c 6A is a eukaryotic member of the Class I cytochrome c family possessing a high structural homology with photosynthetic cytochrome c 6 from cyanobacteria, but structurally and functionally distinct through the presence of a disulfide bond and a heme mid-point redox potential of + 71 mV (vs normal hydrogen electrode). The disulfide bond is part of a loop insertion peptide that forms a cap-like structure on top of the core α-helical fold. We have investigated the contribution of the disulfide bond to thermodynamic stability and (un)folding kinetics in cytochrome c 6A from Arabidopsis thaliana by making comparison with a photosynthetic cytochrome c 6 from Phormidium laminosum and through a mutant in which the Cys residues have been replaced with Ser residues (C67/73S). We find that the disulfide bond makes a significant contribution to overall stability in both the ferric and ferrous heme states. Both cytochromes c 6A and c 6 fold rapidly at neutral pH through an on-pathway intermediate. The unfolding rate for the C67/73S variant is significantly increased indicating that the formation of this region occurs late in the folding pathway. We conclude that the disulfide bridge in cytochrome c 6A acts as a conformational restraint in both the folding intermediate and native state of the protein and that it likely serves a structural rather than a previously proposed catalytic role. © 2011 Elsevier B.V. All rights reserved

Redox-Dependent Stability, Protonation, and Reactivity of Cysteine-Bound Heme Proteins

Cysteine-bound hemes are key components of many enzymes and biological sensors. Protonation (deprotonation) of the Cys ligand often accompanies redox transformations of these centers. To characterize these phenomena, we have engineered a series of Thr78Cys/Lys79Gly/Met80X mutants of yeast cytochrome c (cyt c) in which Cys78 becomes one of the axial ligands to the heme. At neutral pH, the protonation state of the coordinated Cys differs for the ferric and ferrous heme species, with Cys binding as a thiolate and a thiol, respectively. Analysis of redox-dependent stability and alkaline transitions of these model proteins, as well as comparisons to Cys binding studies with the minimalist heme peptide microperoxidase-8, demonstrate that the protein scaffold and solvent interactions play important roles in stabilizing a particular Cys–heme coordination. The increased stability of ferric thiolate compared with ferrous thiol arises mainly from entropic factors. This robust cyt c model system provides access to all four forms of Cys-bound heme, including the ferric thiol. Protein motions control the rates of heme redox reactions, and these effects are amplified at low pH, where the proteins are less stable. Thermodynamic signatures and redox reactivity of the model Cys-bound hemes highlight the critical role of the protein scaffold and its dynamics in modulating redox-linked transitions between thiols and thiolates