68 results match your criteria: "Photodynamics Research Center[Affiliation]"
Plant Cell Physiol
February 2011
Laboratory for Photobiology, Photodynamics Research Center, RIKEN, 519-1399 Aoba, Aramaki, Aoba-ku, Sendai, Miyagi, 980-0845 Japan.
We have developed a plant growth system to analyze water dynamics in the roots of a small model plant, Arabidopsis thaliana, by nuclear magnetic resonance (NMR) microscopic imaging. Using the two-dimensional slice technique, we obtained a series of images with high signal-to-noise ratio indicating the water distribution in the root. To demonstrate light regulation of water transport in the root and involvement of aquaporin gene expression, we visualized the distribution of water in Arabidopsis roots under various light conditions and compared the data with the expression profiles of two aquaporin genes.
View Article and Find Full Text PDFAppl Opt
March 2001
Photodynamics Research Center, RIKEN, 519-1399 Aramaki-Aoba, Sendai 980-0845, Japan.
Using room-temperature parametric oscillation of a LiNbO3 crystal pumped by a Q-switched Nd:YAG laser with a simple configuration, we have realized a widely tunable coherent terahertz- (THz-) wave source in the range between 1 and 3 THz. Inasmuch as the THz wave is affected by total internal reflection at the crystal edge, we used a Si prism coupler to couple out the THz wave. We introduce an arrayed Si-prism coupler that increases the efficiency and decreases the diffraction angle.
View Article and Find Full Text PDFOpt Lett
December 2000
Photodynamics Research Center, RIKEN, 519-1399 Aoba, Aramaki, Aoba-ku, Sendai 980-0868, Japan.
The first known demonstration of tunable terahertz-wave generation by difference-frequency generation of dual signal-wave quasi-phase-matched optical parametric oscillation was performed with periodically poled LiNbO(3) (PPLN) with a series of gratings. An organic ionic salt, 4-dimethylamino-N-methyl-4-stilbazolium-tosylate (DAST), was used as a nonlinear crystal. A compact terahertz-wave source resulted, and changing the temperature of the PPLN permitted the wavelength to be varied from 120 to 160 microm.
View Article and Find Full Text PDFPhys Rev E Stat Nonlin Soft Matter Phys
November 2006
Photodynamics Research Center, The Institute of Physical and Chemical Research (RIKEN), Sendai 980-0845, Japan.
We report the observation of an exotic radiation (unconventional Smith-Purcell radiation) from a one-dimensional photonic crystal. The physical origin of the exotic radiation is direct excitation of the photonic bands by an ultrarelativistic electron beam. The spectrum of the exotic radiation follows photonic bands of a certain parity, in striking contrast to the conventional Smith-Purcell radiation, which shows solely a linear dispersion.
View Article and Find Full Text PDFBiochemistry
March 2006
Laboratory for Photobiology (1), RIKEN Photodynamics Research Center, The Institute of Physical and Chemical Research, 519-1399, Aoba, Sendai 980-0845, Japan.
Blue-light sensing proteins that use FAD (BLUF) are members of a blue-light receptor family that is widely distributed among microorganisms. The Escherichia coli YcgF protein is a BLUF protein consisting of the N-terminal FAD-binding hold (BLUF domain) and the C-terminal EAL domain. The EAL domain of YcgF is predicted to have cyclic-di-GMP phosphodiesterase activity.
View Article and Find Full Text PDFPlant Cell Physiol
March 2006
Laboratory for Photo-Biology (1), Photodynamics Research Center, RIKEN, Sendai, Japan.
Lhl4 encodes a distant relative of light-harvesting Chl-a/b proteins in the green alga Chlamydomonas reinhardtii. Lhl4 mRNA markedly accumulated within 30 min after illumination and in proportion to the light intensity up to a fluence rate much higher than that required for photosynthesis. The high intensity light (HL)-induced accumulation of Lhl4 mRNA required continuous illumination, and the mRNA level rapidly decreased when the cells were placed in the dark.
View Article and Find Full Text PDFPhys Rev Lett
November 2005
RIKEN Photodynamics Research Center, Sendai 980-0845, Japan.
By measuring the very low energy photoemission spectra of the CO/Cu(001) surface with a high resolution, we have found the energy loss components due to inelastic scattering of electrons near the Fermi level by the CO vibrational modes. The main energy loss structure appears as a step at 254 meV below the Fermi edge for 12C16O. An isotope shift of the step to 240 meV was observed when 13C18O was adsorbed.
View Article and Find Full Text PDFJ Phys Chem A
December 2005
Photodynamics Research Center, The Institute of Physical and Chemical Research (RIKEN), 519-1399, Aoba, Aramaki, Aoba-ku, Sendai 980-0845, Japan.
The photochemical reaction mechanisms of model compounds for 4-tert-butyl-1-(4-phenylphenyl)-1-(1,1-dimethylallyl)silacyclohexane are investigated using a complete active space comprised of six electrons in six orbitals with the standard 6-31G(d) basis set. It is concluded that the stereochemistry in the photochemical 1,3-silyl migrations of allylsilanes has a retention preference, in accord with the Woodward-Hoffmann rules. The calculated conical intersection (CI) structure suggests a dissociation path to radicals in addition to a 1,3-shift path.
View Article and Find Full Text PDFBiophys J
March 2006
Photodynamics Research Center, The Institute of Physical and Chemical Research (RIKEN), Miyagi, Japan.
We used direct buckling force measurements with optical traps to determine the flexural rigidity of individual microtubules bound to polystyrene beads. To optimize the accuracy of the measurement, we used two optical traps and antibody-coated beads to manipulate each microtubule. We then applied a new analytical model assuming nonaxial buckling.
View Article and Find Full Text PDFBiochemistry
December 2005
Laboratory for Photo-Biology (1), RIKEN Photodynamics Research Center, The Institute of Physical and Chemical Research, 519-1399 Aoba, Aramaki, Aoba, Sendai 980-0845, Japan.
Changes in structural coupling between the Mn cluster and a putative histidine ligand during the S-state cycling of the oxygen-evolving complex (OEC) have been detected directly by Fourier transform infrared (FTIR) spectroscopy in photosystem (PS) II core particles from the cyanobacterium Synechocystis sp. PCC6803, in which histidine residues were selectively labeled with l-[(15)N(3)]histidine. The bands sensitive to the histidine-specific isotope labeling appeared at 1120-1090 cm(-)(1) in the spectra induced upon the first-, second-, and fourth-flash illumination, for the S(2)/S(1), S(3)/S(2), and S(1)/S(0) differences, at similar frequencies with different sign and/or intensity depending on the respective S-state transitions.
View Article and Find Full Text PDFJ Biol Chem
November 2005
Laboratory for Photo-Biology (1), RIKEN Photodynamics Research Center, The Institute of Physical and Chemical Research, Aramaki, Aoba, Sendai, Japan.
A carboxylate group of D1-Glu-189 in photosystem II has been proposed to serve as a direct ligand for the manganese cluster. Here we constructed a mutant that eliminates the carboxylate by replacing D1-Glu-189 with Gln in the cyanobacterium Synechocystis sp. PCC 6803, and we examined the resulting effects on the structural and functional properties of the oxygen-evolving complex (OEC) in photosystem II.
View Article and Find Full Text PDFPhotosynth Res
June 2005
Laboratory for Photo-Biology (1), RIKEN Photodynamics Research Center, 519-1399 Aoba, Aramaki, Aoba, Sendai 980-0845, Japan.
Structural roles of functional Ca2+ and Cl- ions in photosynthetic oxygen-evolving complexes (OEC) were studied using low- (640-350 cm-1) and mid- (1800-1200 cm-1) frequency S2/S1 Fourier transform infrared (FTIR) difference spectroscopy. Studies using highly active Photosystem (PS) II core particles from spinach enabled the detection of subtle spectral changes. Ca2+-depleted and Ca2+-reconstituted particles produced very similar mid- and low-frequency spectra.
View Article and Find Full Text PDFJ Bacteriol
July 2005
Laboratory for Photo-Biology, RIKEN Photodynamics Research Center, The Institute of Physical and Chemical Research, Aramaki, Aoba, Sendai, Japan.
Bicarbonate stimulates the activities of several class III adenylyl cyclases studied to date. However, we show here that bicarbonate decreased V(max) and substrate affinity in Cya1, a major adenylyl cyclase in the cyanobacterium Synechocystis sp. strain PCC 6803.
View Article and Find Full Text PDFBiochemistry
June 2005
Laboratory for Photo-Biology (I), RIKEN Photodynamics Research Center, Aoba, Sendai, Miyagi 980-0845, Japan. kojihase@ postman.riken.go.jp
The primary donor chlorophyll (Chl) of photosystem II (PSII), P680, has an extremely high oxidation redox potential (E(ox)) of approximately 1.2 V, which is essential for photosynthetic water oxidation. The mechanism for achieving a high potential such as that of P680 has been one of the central questions in photosynthesis research.
View Article and Find Full Text PDFBiochemistry
May 2005
Laboratory for Photo-Biology (1), RIKEN Photodynamics Research Center, Institute of Physical and Chemical Research, 519-1399 Aoba, Aramaki, Aoba, Sendai 980-0845, Japan.
In photosynthetic water oxidation, two water molecules are converted to an oxygen molecule through five reaction intermediates, designated S(n) (n = 0-4), at the catalytic Mn cluster of photosystem II. To understand the mechanism of water oxidation, changes in the chemical nature of the substrate water as well as the Mn cluster need to be defined during S-state cycling. Here, we report for the first time a complete set of Fourier transform infrared difference spectra during S-state cycling in the low-frequency (670-350 cm(-1)) region, in which interactions between the Mn cluster and its ligands can be detected directly, in PS II core particles from Thermosynechococcus elongatus.
View Article and Find Full Text PDFOpt Lett
May 2005
Photophysics Laboratory, Photodynamics Research Center, RIKEN, 519-1399, Aoba, Aramaki, Aoba-ku, Sendai, Miyagi 980-0845, Japan.
A bent photonic crystal waveguide was fabricated by use of a lattice pattern of a circular photonic crystal that allowed high transmission for a broad band of wavelengths with a small radius of curvature at a bend. The waveguide was fabricated by use of alumina rods with a diameter of 3 mm. Windows of high transmission as a result of waveguiding were observed near 9 and 15 GHz.
View Article and Find Full Text PDFBiochemistry
February 2005
Laboratory for Photobiology (1), RIKEN Photodynamics Research Center, The Institute of Physical and Chemical Research, 519-1399, Aoba, Sendai 980-0845, Japan.
AppA is a new class blue-light receptor controlling photosynthesis gene expression in the purple bacterium Rhodobacter sphaeroides and retains a characteristic flavin adenine dinucleotide (FAD)-binding domain named the "sensor of blue light using FAD" (BLUF). AppA functions as an antirepressor controlling transcription of photosynthesis genes through the direct association with a transcriptional repressor PpsR in a blue-light-dependent manner [Masuda and Bauer (2002) Cell 110, 613-623]. Illumination of AppA induces a red shift in the UV-visible absorption of FAD, which results in a signaling state of AppA.
View Article and Find Full Text PDFPlant Cell Physiol
January 2005
Laboratory for Photo-Biology (I), RIKEN Photodynamics Research Center, The Institute of Physical and Chemical Research, 519-1399 Aoba, Aoba, Sendai, 980-0845 Japan.
Slr1694 is a BLUF (sensor of blue light using flavin adenine dinucleotide) protein and a putative photoreceptor in the cyanobacterium Synechocystis sp. PCC6803. Illumination of Slr1694 induced a signaling light state concurrent with a red shift in the UV-visible absorption of flavin, and formation of the bands from flavin and apo-protein in the light-minus-dark Fourier transform infrared (FTIR) difference spectrum.
View Article and Find Full Text PDFBiochemistry
November 2004
Laboratory for Photo-Biology, RIKEN Photodynamics Research Center, The Institute of Physical and Chemical Research, 519-1399 Aoba, Aramaki, Aoba, Sendai 980-0845, Japan.
Slr1694 in Synechocystis sp. PCC6803 is a family of blue-light photoreceptors based on flavin adenine dinucleotide (FAD) called BLUF (sensor of blue light using FAD) proteins, which include AppA from Rhodobacter sphaeroides and PAC from Euglena gracilis. Illumination of dark-state Slr1694 at 15 degrees C reversibly induced a signaling light state characterized by the red shift in the UV-visible spectrum and by the light-induced Fourier transform infrared (FTIR) difference spectrum for structural changes of a bound flavin and apo protein.
View Article and Find Full Text PDFBiochemistry
November 2004
Laboratory for Photo-Biology (1), RIKEN Photodynamics Research Center, The Institute of Physical and Chemical Research (RIKEN), 519-1399 Aoba, Aramaki, Aoba, Sendai 980-0845, Japan.
A free alpha-COO(-) in the C-terminal alanine-344 (Ala344) in the D1 protein of photosystem II is thought to be responsible for ligating the Mn cluster. The effects of the side group of the C-terminus of the D1 protein on the functional and structural properties of the oxygen-evolving complex (OEC) were comprehensively studied by replacing Ala344 with glycine (Gly), valine (Val), aspartate (Asp), or asparagine (Asn). All the mutants grew photoautotrophically under low-light conditions with lower O(2) evolution activity depending on the mutants when compared with the activity of the control wild type.
View Article and Find Full Text PDFJ Biol Chem
January 2005
Laboratory for Photo-Biology (1), RIKEN Photodynamics Research Center, The Institute of Physical and Chemical Research, 519-1399 Aoba, Aramaki, Aoba, Sendai 980-0845, Japan.
Changes in the chemical structure of alpha-carboxylate of the D1 C-terminal Ala-344 during S-state cycling of photosynthetic oxygen-evolving complex were selectively measured using light-induced Fourier transform infrared (FTIR) difference spectroscopy in combination with specific [(13)C]alanine labeling and site-directed mutagenesis in photosystem II core particles from Synechocystis sp. PCC 6803. Several bands for carboxylate symmetric stretching modes in an S(2)/S(1) FTIR difference spectrum were affected by selective (13)C labeling of the alpha-carboxylate of Ala with l-[1-(13)C]alanine, whereas most of the isotopic effects failed to be induced in a site-directed mutant in which Ala-344 was replaced with Gly.
View Article and Find Full Text PDFJ Exp Bot
January 2005
Photodynamics Research Center, RIKEN (The Institute of Physical and Chemical Research), Sendai 980-0845, Japan.
In order to reveal any roles played by stems and roots of herbaceous plants in responding to the surrounding light environment, the optical properties of the stem and root tissues of 18 herbaceous species were investigated. It was found that light was able to penetrate through to the interior of the stem and was then conducted towards the roots. Light conduction was carried out within the internodes and across the nodes of the stem, and then in the roots from the tap root to lateral roots.
View Article and Find Full Text PDFFEBS Lett
November 2004
Laboratory for Photo-Biology (1), RIKEN Photodynamics Research Center, The Institute of Physical and Chemical Research, 519-1399 Aramaki, Aoba, Sendai 980-0845, Japan.
We report herein the biochemical properties of an adenylyl cyclase, Cya1, from the cyanobacterium Synechocystis sp. PCC 6803. Heterologously expressed Cya1 catalyzed cyclic AMP formation with a Km for ATP of approximately 2.
View Article and Find Full Text PDFPlant Cell Physiol
September 2004
Laboratory for Photo-Biology (1), Photodynamics Research Center, RIKEN (The Institute of Physical and Chemical Research), Sendai, 980-0845 Japan.
We identified four Lhc-like genes (Lhl) encoding proteins that are distant relatives of light-harvesting chlorophyll a/b-binding (LHC) proteins in the green alga Chlamydomonas reinhardtii. Their mRNA levels after transfer from low-intensity light to high-intensity light (HL) were examined and compared with those of Lhc genes encoding LHC proteins of PSII. The transfer caused a decrease in the mRNA level of Lhl3, a homolog of Arabidopsis thaliana Lil3, within 2 h, followed by gradual restoration depending on the intensity of HL.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
September 2004
Photodynamics Research Center, The Institute of Physical and Chemical Research (RIKEN), 519-1399 Aoba, Aramaki, Aoba-ku, Sendai 980-0845, Japan.