Terahertz Response of Acoustically-Driven Optical Phonons

The manipulation of TO-phonon polaritons and the terahertz (THz) light field associated with them by means of an ultra-sound acoustic wave is proposed and illustrated by calculating the TO-phonon-mediated THz response of acoustically-pumped CuCl and TlCl crystals. We show the high-contrast acoustically-induced change of the THz reflectivity alongside with multiple THz Bragg replicas, which are associated with the infrared-active TO-phonon resonance driven by the ultrasonic wave. The effect, which stems from phonon anharmonicity, refers to an operating acoustic intensity I_ac ~ 1-100 kW/cm^2 and frequency nu_ac ~ 0.1 - 1 GHz, with possible applications in THz spectroscopy.Comment: 10 pages, 4 figure

Resonant acousto-optics in the terahertz range: TO-phonon polaritons driven by an ultrasonic wave

The resonant acousto-optic effect is studied both analytically and numerically in the terahertz range where the transverse-optical (TO) phonons play the role of a mediator which strongly couples the ultrasound and light fields. A propagating acoustic wave interacts with the TO phonons via anharmonic channels and opens band gaps in the TO-phonon polariton energy dispersion that results in pronounced Bragg scattering and reflection of the incoming light. The separation in frequency of different Bragg replicas, which is at the heart of acousto-optics, allows us to study the resonant acousto-optic effect in the most simple and efficient geometry of collinear propagation of electromagnetic and ultrasonic waves. The acoustically induced energy gaps, Bragg reflection spectra, and the spatial distribution of the electric field and polarization are calculated for CuCl parameters, in a wide range of frequencies and intensities of the pumping acoustic wave. Our results show drastic changes in terahertz spectra of semiconductor crystals that opens the way for efficient and accessible manipulation of their infrared properties, by tuning the parameters of the acoustic wave.Comment: 20 pages, 14 figure

Structural divergence of paralogous S components from ECF-type ABC transporters

Energy coupling factor (ECF) proteins are ATP-binding cassette transporters involved in the import of micronutrients in prokaryotes. They consist of two nucleotide-binding subunits and the integral membrane subunit EcfT, which together form the ECF module and a second integral membrane subunit that captures the substrate (the S component). Different S components, unrelated in sequence and specific for different ligands, can interact with the same ECF module. Here, we present a high-resolution crystal structure at 2.1 Å of the biotin-specific S component BioY from Lactococcus lactis. BioY shares only 16% sequence identity with the thiamin-specific S component ThiT from the same organism, of which we recently solved a crystal structure. Consistent with the lack of sequence similarity, BioY and ThiT display large structural differences (rmsd = 5.1 Å), but the divergence is not equally distributed over the molecules: The S components contain a structurally conserved N-terminal domain that is involved in the interaction with the ECF module and a highly divergent C-terminal domain that binds the substrate. The domain structure explains howthe S components with large overall structural differences can interact with the same ECF module while at the same time specifically bind very different substrates with subnanomolar affinity. Solitary BioY (in the absence of the ECF module) is monomeric in detergent solution and binds D-biotin with a high affinity but does not transport the substrate across the membrane.

Functional interactions between the subunits of the lactose transporter from Streptococcus thermophilus

Although the quaternary state has been assessed in detail for only a few members of the major facilitator superfamily (MFS), it is clear that multiple oligomeric states are represented within the MFS. One of its members, the lactose transporter LacS from Streptococcus thermophilus assumes a dimeric structure in the membrane and in vitro analysis showed functional interactions between both subunits when proton motive force (Delta p)-driven transport was assayed. To study the interactions in further detail, a covalent dimer was constructed consisting of in tandem fused LacS subunits. These covalent dimers, composed of active and completely inactive subunits, were expressed in Escherichia coli, and initial rates of Delta p-driven lactose uptake and lactose counterflow were determined. We now show that also in vivo, both subunits interact functionally; that is, partial complementation of the inactive subunit was observed for both transport modes. Thus, both subunits interact functionally in Delta p-driven uptake and in counterflow transport. In addition, analysis of in tandem fused LacS subunits containing one regulatory LacS-IIA domain showed that regulation is primarily an intramolecular event. (c) 2005 Elsevier Ltd. All rights reserved

Identification of the dimer interface of the lactose transport protein from Streptococcus thermophilus

The lactose transporter from Streptococcus thermophilus catalyses the symport of galactosides and protons. The carrier domain of the protein harbours the contact sites for dimerization, and the individual subunits in the dimer interact functionally during the transport reaction. As a first step towards the elucidation of the mechanism behind the cooperation between the subunits, regions involved in the dimer interface were determined by oxidative and chemical cross-linking of 12 cysteine substitution mutants. Four positions in the protein were found to be susceptible to intermolecular cross-linking. To ensure that the observed cross-links were not the result of randomly colliding particles, the cross-linking was studied in samples in which either the concentration of LacS in the membrane was varied or the oligomeric state was manipulated. These experiments showed that the cross-links were formed specifically within the dimer. The four regions of the protein located at the dimer interface are close to the extracellular ends of transmembrane segments V and VIII and the intracellular ends of transmembrane segments VI and VII

Ultrasonic control of terahertz radiation via lattice anharmonicity in LiNbO3

We propose a novel tunable terahertz (THz) filter using the resonant acousto-optic (RAO) effect. We present a design based on a transverse optical (TO) phonon mediated interaction between a coherent acoustic wave and the THz field in LiNbO3. We predict a continuously tunable range of the filter up to 4 THz via the variation of the acoustic frequency between 0.1 and 1 GHz. The RAO effect in this case is due to cubic and quartic anharmonicities between TO phonons and the acoustic field. The effect of the interference between the anharmonicities is also discussed.Comment: 3 pages, 4 figure