Hyotcherl Ihee

A belt-shaped, blue luminescent, and semiconducting covalent organic framework.

From a synthetic viewpoint,COFs are attractive motifs since they allow total control overstructural parameters,including composition and porosity,after appropriate topological design. Most studies to datehave focused on the development of synthetic methodologieswith the aim of optimizing pore size and surface area.

A Photoconductive Covalent Organic Framework: Self‐Condensed Arene Cubes Composed of Eclipsed 2D Polypyrene Sheets for Photocurrent Generation

Covalent organic frameworks (COFs) are porous crystalline materials with predesignable 2D and 3D polymer structures. Owing to the covalent linkage of the components, as well as the elaborate control of structural parameters, including porosity and composition, COFs are promising for the design of tailor-made porous materials for gas storage. 7,8] We recently reported the cocondensation of triphenylene and pyrene monomers to create a semiconducting pconjugated COF (TP-COF). The well-defined crystalline structure of COFs should have a high probability of forming a conduction path that transports charge carriers across the framework. We are interested in the synthesis of photofunctional COFs, in particular a photoconductive COF, which would require photoinduced carrier generation and carrier transportation in the framework. Crystal engineering has demonstrated that high-quality single crystals of certain p-conjugated arenes are photoconductive as the result of exciton migration over the lattice followed by charge separation at the molecule–electrode interface. To fulfill this prerequisite, we investigated an arene-based COF, which should retain a crystal-lattice-like highly ordered arene arrangement, absorb photons in the visible region, and be robust under irradiation. Herein, we report the first example of a photoconductive COF, in which sheets composed of arene building blocks lie above one another in an eclipsed arrangement (Figure 1, PPyCOF). We chose the self-condensation of pyrenediboronic acid (Figure 1a, PDBA) as the polymerization reaction for structure formation, as we anticipated that this reaction would lead to the integration of pyrene units on edges and

Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering

We demonstrate tracking of protein structural changes with time-resolved wide-angle X-ray scattering (TR-WAXS) with nanosecond time resolution. We investigated the tertiary and quaternary conformational changes of human hemoglobin under nearly physiological conditions triggered by laser-induced ligand photolysis. We also report data on optically induced tertiary relaxations of myoglobin and refolding of cytochrome c to illustrate the wide applicability of the technique. By providing insights into the structural dynamics of proteins functioning in their natural environment, TR-WAXS complements and extends results obtained with time-resolved optical spectroscopy and X-ray crystallography.

Conjugated organic framework with three-dimensionally ordered stable structure and delocalized π clouds

Covalent organic frameworks are a class of crystalline organic porous materials that can utilize π–π-stacking interactions as a driving force for the crystallization of polygonal sheets to form layered frameworks and ordered pores. However, typical examples are chemically unstable and lack intrasheet π-conjugation, thereby significantly limiting their applications. Here we report a chemically stable, electronically conjugated organic framework with topologically designed wire frameworks and open nanochannels, in which the π conjugation-spans the two-dimensional sheets. Our framework permits inborn periodic ordering of conjugated chains in all three dimensions and exhibits a striking combination of properties: chemical stability, extended π-delocalization, ability to host guest molecules and hole mobility. We show that the π-conjugated organic framework is useful for high on-off ratio photoswitches and photovoltaic cells. Therefore, this strategy may constitute a step towards realizing ordered semiconducting porous materials for innovations based on two-dimensionally extended π systems.

Single nanowire on a film as an efficient SERS-active platform.

Fabricating well-defined and highly reproducible platforms for surface-enhanced Raman scattering (SERS) is very important in developing practical SERS sensors. We report a novel SERS platform composed of a single metallic nanowire (NW) on a metallic film. Optical excitation of this novel sandwich nanostructure provides a line of SERS hot spots (a SERS hot line) at the gap between the NW and the film. This single nanowire on a film (SNOF) architecture can be easily fabricated, and the position of hot spots can be conveniently located in situ by using an optical microscope during the SERS measurement. We show that high-quality SERS spectra from benzenethiol, brilliant cresyl blue, and single-stranded DNA can be obtained on a SNOF with reliable reproducibility, good time stability, and excellent sensitivity, and thus, SNOFs can potentially be employed as effective SERS sensors for label-free biomolecule detection. We also report detailed studies of polarization- and material-dependent SERS enhancement of the SNOF structure.

Role of Water in Directing Diphenylalanine Assembly into Nanotubes and Nanowires

[*] Prof. H. Ihee, J. Kim, Dr. J. Choi Center for Time-Resolved Diffraction, Department of Chemistry Graduate School of Nanoscience & Technology (WCU), KAIST 335 Gwahangno, Yuseong-gu Daejeon, 305-701 (Republic of Korea) E-mail: hyotcherl.ihee@kaist.ac.kr Prof. S. O. Kim, T. H. Han, J. S. Park Department of Materials Science and Engineering (BK21) KAIST Institute for the Nanocentury, KAIST 335 Gwahangno, Yuseong-gu Daejeon, 305-701 (Republic of Korea) E-mail: sangouk.kim@kaist.ac.kr Dr. Y. Kim Korea Research Institute of Standards and Science P.O. Box 102, Yuseong-gu Daejeon, 305-340 (Republic of Korea)

Volume-conserving trans – cis isomerization pathways in photoactive yellow protein visualized by picosecond X-ray crystallography

Trans-to-cis isomerization, the key reaction in photoactive proteins, cannot usually occur through the standard one-bond-flip mechanism. Due to spatial constraints imposed by a protein environment, isomerization is likely to proceed via a “volume-conserving” mechanism in which highly-choreographed atomic motions are expected, the details of which have not yet been directly observed. Here we employ time-resolved X-ray crystallography to structurally visualize isomerization of the p-coumaric acid chromophore in photoactive yellow protein with 100 picosecond time resolution and 1.6 Å spatial resolution. The structure of the earliest intermediate (IT) resembles a highly-strained transition state in which the torsion angle is located halfway between the trans and cis isomers. The reaction trajectory of IT bifurcates into two structurally distinct cis intermediates via hula-twist and bicycle-pedal pathways. The bifurcating reaction pathways can be controlled by weakening the hydrogen bond between the chromophore and an adjacent residue via E46Q mutation, which switches off the bicycle-pedal pathway.

Steering Epitaxial Alignment of Au, Pd, and AuPd Nanowire Arrays by Atom Flux Change

We have synthesized epitaxial Au, Pd, and AuPd nanowire arrays in vertical or horizontal alignment on a c-cut sapphire substrate. We show that the vertical and horizontal nanowire arrays grow from half-octahedral seeds by the correlations of the geometry and orientation of seed crystals with those of as-grown nanowires. The alignment of nanowires can be steered by changing the atom flux. At low atom deposition flux vertical nanowires grow, while at high atom flux horizontal nanowires grow. Similar vertical/horizontal epitaxial growth is also demonstrated on SrTiO(3) substrates. This orientation-steering mechanism is visualized by molecular dynamics simulations.

Visualizing solution-phase reaction dynamics with time-resolved X-ray liquidography.

Most chemical reactions occur in solution, and complex interactions between solute and solvent influence the rich chemistry of these processes. To track time-dependent processes in such reactions, researchers often use time-resolved spectroscopy. In these experiments, an optical pulse (pump) initiates a reaction, and another time-delayed optical pulse (probe) monitors the progress of the reaction. However, because of the wavelength range of the probe light used in these experiments, from infrared to ultraviolet, researchers cannot directly determine detailed structural information such as the bond lengths and bond angles of reaction intermediates. In addition, not all intermediates might be sensitive to the spectroscopic signal chosen for the experiment. This Account describes time-resolved X-ray liquidography (TRXL), a technique that overcomes these problems. In this technique, we replace the optical probe with the diffraction of hard X-ray pulses emitted from a synchrotron source. In TRXL, diffraction signals are sensitive to all chemical species simultaneously. In addition, each chemical species has a characteristic diffraction signal, a fingerprint, that we calculate from its three-dimensional atomic coordinates. Because, X-rays scatter from all atoms in the solution sample, including both the solute and the solvent, the analysis of TRXL data can track not only the reaction pathways of the solute molecules but also the solvent behavior and the solute-solvent arrangement, thus providing a global picture of the reactions. We have used TRXL to study structural dynamics and spatiotemporal kinetics of many molecular systems including diatomic molecules, haloalkanes, organometallic complexes, and protein molecules over timescales from picoseconds to milliseconds. We have observed that TRXL data adds to and, in some cases, contradicts results from time-resolved spectroscopy. For example, TRXL has shown that the reaction intermediates upon C-I bond dissociation in C(2)H(4)I(2) and C(2)F(4)I(2) have completely different structures and corresponding subsequent reaction pathways, underscoring the dramatic effect of the fluorine substitution. We have also used TRXL to identify a new reaction intermediate of the photolysis of Ru(3)(CO)(12) that has no bridging carbonyl groups. Though not detected by time-resolved infrared spectroscopy, this intermediate predominates based on the TRXL data. In looking at the quaternary conformational changes of hemoglobin, TRXL analysis suggests a faster transition than was suggested by optical spectroscopy. The time resolution of TRXL is currently limited by the X-ray pulse width available from synchrotron sources ( approximately 100 ps). The resolution should improve to 100 fs or better with X-ray free electron lasers. With this higher resolution, real time observation of ultrafast chemical events such as bond-breaking and bond-making will be possible.

Protein Structural Dynamics of Photoactive Yellow Protein in Solution Revealed by Pump–Probe X-ray Solution Scattering

Photoreceptor proteins play crucial roles in receiving light stimuli that give rise to the responses required for biological function. However, structural characterization of conformational transition of the photoreceptors has been elusive in their native aqueous environment, even for a prototype photoreceptor, photoactive yellow protein (PYP). We employ pump-probe X-ray solution scattering to probe the structural changes that occur during the photocycle of PYP in a wide time range from 3.16 μs to 300 ms. By the analysis of both kinetics and structures of the intermediates, the structural progression of the protein in the solution phase is vividly visualized. We identify four structurally distinct intermediates and their associated five time constants and reconstructed the molecular shapes of the four intermediates from time-independent, species-associated difference scattering curves. The reconstructed structures of the intermediates show the large conformational changes such as the protrusion of N-terminus, which is restricted in the crystalline phase due to the crystal contact and thus could not be clearly observed by X-ray crystallography. The protrusion of the N-terminus and the protein volume gradually increase with the progress of the photocycle and becomes maximal in the final intermediate, which is proposed to be the signaling state. The data not only reveal that a common kinetic mechanism is applicable to both the crystalline and the solution phases, but also provide direct evidence for how the sample environment influences structural dynamics and the reaction rates of the PYP photocycle.