Effective surface conductivity of optical hyperbolic metasurfaces: from far-field characterization to surface wave analysis

Abstract Metasurfaces offer great potential to control near- and far-fields through engineering optical properties of elementary cells or meta-atoms. Such perspective opens a route to efficient manipulation of the optical signals both at nanoscale and in photonics applications. In this paper we show that a local surface conductivity tensor well describes optical properties of a resonant plasmonic hyperbolic metasurface both in the far-field and in the near-field regimes, where spatial dispersion usually plays a crucial role. We retrieve the effective surface conductivity tensor from the comparative analysis of experimental and numerical reflectance spectra of a metasurface composed of elliptical gold nanoparticles. Afterwards, the restored conductivities are validated by semi-analytic parameters obtained with the nonlocal discrete dipole model with and without interaction contribution between meta-atoms. The effective parameters are further used for the dispersion analysis of surface plasmons localized at the metasurface. The obtained effective conductivity describes correctly the dispersion law of both quasi-TE and quasi-TM plasmons in a wide range of optical frequencies as well as the peculiarities of their propagation regimes, in particular, topological transition from the elliptical to hyperbolic regime with eligible accuracy. The analysis in question offers a simple practical way to describe properties of metasurfaces including ones in the near-field zone with effective conductivity tensor extracting from the convenient far-field characterization

Light-Induced Thiol Oxidation of Recoverin Affects Rhodopsin Desensitization

The excessive light illumination of mammalian retina is known to induce oxidative stress and photoreceptor cell death linked to progression of age-related macular degeneration. The photochemical damage of photoreceptors is suggested to occur via two apoptotic pathways that involve either excessive rhodopsin activation or constitutive phototransduction, depending on the light intensity. Both pathways are dramatically activated in the absence of rhodopsin desensitization by GRK1. Previously, we have shown that moderate illumination (halogen lamp, 1,500 lx, 1–5 h) of mammalian eyes provokes disulfide dimerization of recoverin, a calcium-dependent regulator of GRK1. Here, we demonstrate under in vivo conditions that both moderate long-term (metal halide lamp, 2,500 lx, 14 h, rat model) and intense short-term (halogen lamp, 30,000 lx for 3 h, rabbit model) illumination of the mammalian retina are accompanied by accumulation of disulfide dimer of recoverin. Furthermore, in the second case we reveal alternatively oxidized derivatives of the protein, apparently including its monomer with sulfinic group. Histological data indicate that thiol oxidation of recoverin precedes apoptosis of photoreceptors. Both disulfide dimer and oxidized monomer (or oxidation mimicking C39D mutant) of recoverin exhibit lowered α-helical content and thermal stability of their apo-forms, as well as increased Ca2+ affinity. Meanwhile, the oxidized monomer and C39D mutant of recoverin demonstrate impaired ability to bind photoreceptor membranes and regulate GRK1, whereas disulfide dimer exhibits notably improved membrane binding and GRK1 inhibition in absence of Ca2+. The latter effect is expected to slow down rhodopsin desensitization in the light, thereby favoring support of the light-induced oxidative stress, ultimately leading to photoreceptor apoptosis. Overall, the intensity and duration of illumination of the retina affect thiol oxidation of recoverin likely contributing to propagation of the oxidative stress and photoreceptor damage

Mapping electromagnetic fields near a subwavelength hole

We study, both experimentally and theoretically, the scattering of electromagnetic waves by a subwavelength hole fabricated in a thin metallic film. We employ the scanning near-field optical microscopy in order to reconstruct experimentally the full three-dimensional structure of the electromagnetic fields in the vicinity of the hole. We observe an interference of all excited waves with an incident laser beam which allows us to gain the information about the wave phases. Along with the well-known surface plasmon polaritons propagating primarily in the direction of the incident beam polarization, we observe the free-space radiation diffracted by the hole. We compare the experimental results with the fields of pure electric and pure magnetic dipoles as well as with direct numerical simulations. We confirm that a single hole in a thin metallic film excited at the normal incidence manifests itself as an effective magnetic dipole in the visible spectral range

Potassium Trifluorotris(pentafluoroethyl)phosphate

A transparent white crystalline product, K[(C2F5)3PF3] (KFAP), has been synthesized via a one-pot route. Difluorotris(pentafluoroethyl)phosphorane was reacted first with aqueous HF then with K2CO3 or KHCO3 in a solution. Isolation of the intermediate, tris(pentafluoroethyl)trifluorophosphoric acid H[(C2F5)3PF3] (HFAP), was not carried out. The salt has been characterised by powder and single crystal X-ray diffraction. The single-crystal structure shows a monoperiodic coordination polymer involving K∙∙∙F bridging interactions to be present. The thermal characteristics and behaviour of KFAP have been established by simultaneous TGA-DSC measurements

Effects of Mutations in The Calcium-binding Sites of Recoverin on Its Calcium Affinity: Evidence for Successive Filling of The Calcium Binding Sites

A molecule of the photoreceptor Ca2+-binding protein recoverin contains four potential EF-hand Ca2+-binding sites, of which only two, the second and the third, are capable of binding calcium ions. We have studied the effects of substitutions in the second, third and fourth EF-hand sites of recoverin on its Ca2+-binding properties and some other characteristics, using intrinsic fluorescence, circular dichroism spectroscopy and differential scanning microcalorimetry. The interaction of the two operating binding sites of wild-type recoverin with calcium increases the protein\u27s thermal stability, but makes the environment around the tryptophan residues more flexible. The amino acid substitution in the EF-hand 3 (E121Q) totally abolishes the high calcium affinity of recoverin, while the mutation in the EF-hand 2 (E85Q) causes only a moderate decrease in calcium binding. Based on this evidence, we suggest that the binding of calcium ions to recoverin is a sequential process with the EF-hand 3 being filled first. Estimation of Ca2+-binding constants according to the sequential binding scheme gave the values 3.7 × 106 and 3.1 × 105 M–1 for third and second EF-hands, respectively. The substitutions in the EF-hand 2 or 3 (or in both the sites simultaneously) do not disturb significantly either tertiary or secondary structure of the apo-protein. Amino acid substitutions, which have been designed to restore the calcium affinity of the EF-hand 4 (G160D, K161E, K162N, D165G and K166Q), increase the calcium capacity and affinity of recoverin but also perturb the protein structure and decrease the thermostability of its apo-form

Recoverin Is a Zinc-binding Protein

Recoverin is an N-myristoylated 23 kDa calcium-binding protein from retina, which modulates the Ca2+-sensitive deactivation of rhodopsin via Ca2+-dependent inhibition of rhodopsin kinase. It was shown by intrinsic and bis-ANS probe fluorescence, circular dichroism, and differential scanning calorimetry that myristoylated recombinant recoverin interacts specifically with zinc ions. Similar to the calcium binding, the binding of zinc to Ca2+-loaded recoverin additionally increases its α-helical content, hydrophobic surface area, and environmental mobility/polarity of its tryptophan residues. In contrast to the calcium binding, the binding of zinc decreases thermal stability of the Ca2+-loaded protein. Zn2+-titration of recoverin, traced by bis-ANS fluorescence, reveals binding of a single Zn2+ ion per protein molecule. It was shown that the double-mutant E85Q/E121Q with inactivated Ca2+-binding EF-hands 2 and 3 (Alekseev, A. M.; Shulga-Morskoy, S. V.; Zinchenko, D. V.; Shulga-Morskaya, S. A.; Suchkov, D. V.; Vaganova, S. A.; Senin, I. I.; Zargarov, A. A.; Lipkin, V. M.; Akhtar, M.; Philippov, P. P. FEBS Lett.1998, 440, 116−118), which can be considered as an analogue of the apo-protein, binds Zn2+ ion as well. Apparent zinc equilibrium binding constants evaluated from spectrofluorimetric Zn2+-titrations of the protein are 1.4 × 105 M-1 (dissociation constant 7.1 μM) for Ca2+-loaded wild-type recoverin and 3.3 × 104 M-1 (dissociation constant 30 μM) for the E85Q/E121Q mutant (analogue of apo-recoverin). Study of the binding of wild-type recoverin to ROS membranes showed a zinc-dependent increase of its affinity for the membranes, without regard to calcium content, suggesting further solvation of a protein myristoyl group upon Zn2+ binding. Possible implications of these findings to the functioning of recoverin are discussed

Point Amino Acid Substitutions in The Ca\u3csup\u3e2+\u3c/sup\u3e-binding Sites of Recoverin: III. A Mutant with The Fourth Reconstructed Ca\u3csup\u3e2+\u3c/sup\u3e-binding Site

Unlike wild type recoverin with only two (the second and the third) functioning Ca+2-binding sites out of four potential ones, the +EF4 mutant contains a third active Ca+2-binding site. This site was reconstructed from the fourth potential Ca+2-binding domain by the introduction of several amino acid substitutions in it by site-directed mutagenesis. The effect of these mutations in the fourth potential Ca+2-binding site of myristoylated recoverin on the structural features and conformational stability of the protein was studied by fluorimetry and circular dichroism. The apoform of the resulting mutant (free of Ca2+ ions) was shown to have a higher calcium capacity, significantly lower thermal stability, and noticeably different secondary and tertiary structures as compared with the apoform of wild-type recoverin