Improving the corrosion resistance of silicon carbide for fuel in BWR environments by using a metal coating

Ishibashi, Ryo*; Tanabe, Shigetada*; Kondo, Takao*; Yamashita, Shinichiro; Nagase, Fumihisa

Proceedings of 2017 Water Reactor Fuel Performance Meeting (WRFPM 2017) (USB Flash Drive), 10 Pages, 2017/09

http://www.wrfpm2017.org/upload/draft_file/F-177-PD1.pdf

For improving the corrosion resistance of silicon carbide (SiC) in boiling-water-reactor environments, corrosion-resistant coatings on SiC were evaluated. Due to its hydrogen-generation rate and reaction heat being lower than those of conventional Zircaloy, SiC is expected to be an appropriate material for accident-tolerant fuels. However, there are still many critical issues with the practical application of SiC fuel cladding and fuel channel boxes, one of which is hydrothermal corrosion. Silicon carbide is chemically stable, but silicon oxide formed by oxidation of SiC dissolves in high temperature water. Although the rate of SiC dissolution is very small, the dissolution must be suppressed to comply with regulations for dissolved silica concentration in reactor coolant. In this study, the corrosion behavior of candidate coatings for SiC substrates were evaluated before and after exposure to unirradiated high-purity-water environments.

Nucleoside diphosphate kinase from psychrophilic sp. AS-131 isolated from Antarctic Ocean

Yonezawa, Yasushi*; Nagayama, Aiko*; Tokunaga, Hiroko*; Ishibashi, Matsujiro*; Arai, Shigeki; Kuroki, Ryota; Watanabe, Keiichi*; Arakawa, Tsutomu*; Tokunaga, Masao*

Protein Journal, 34(4), p.275 - 283, 2015/08

https://doi.org/10.1007/s10930-015-9623-0

Nucleoside diphosphate kinase isolated from psychrophilic sp. AS-131 (ASNDK) was expressed in and purified to homogeneity. Comparing to mesophilic NDK isolated from , ASNDK exhibited highly elevated thermolability: (1) expression at 37C as a denatured insoluble form, and (2) 30C lower optimum temperature of enzymatic activity. The subunit structure of ASNDK was suggested to be dimer, as in NDKs isolated from moderate halophiles.

Structural characteristics of alkaline phosphatase from the moderately halophilic bacterium sp.593

Arai, Shigeki; Yonezawa, Yasushi*; Ishibashi, Matsujiro*; Matsumoto, Fumiko*; Adachi, Motoyasu; Tamada, Taro; Tokunaga, Hiroko*; Blaber, M.; Tokunaga, Masao*; Kuroki, Ryota

Acta Crystallographica Section D, 70(3), p.811 - 820, 2014/03

https://doi.org/10.1107/S1399004713033609

In order to clarify the structural basis of halophilic characteristics of an alkaline phosphatase derived from the moderate halophile sp.593 (HaAP), the tertiary structure of HaAP was determined to 2.1 resolution by X-ray crystallography. Structural properties of surface negative charge and core hydrophobicity are shown to be intermediate between halophile and non-halophile characteristics, and may explain the unique functional adaptation to a wide-range of salt concentration.

Mizunami Underground Research Laboratory Project, Annual report for fiscal year 2011

Kunimaru, Takanori; Mikake, Shinichiro; Nishio, Kazuhisa; Tsuruta, Tadahiko; Matsuoka, Toshiyuki; Ishibashi, Masayuki; Sasao, Eiji; Hikima, Ryoichi; Tanno, Takeo; Sanada, Hiroyuki; et al.

JAEA-Review 2013-018, 169 Pages, 2013/09

JAEA-Review-2013-018.pdf:15.71MB

Japan Atomic Energy Agency (JAEA) at Tono Geoscience Center (TGC) is pursuing a geoscientific research and development project namely the Mizunami Underground Research Laboratory (MIU) Project in crystalline rock environment in order to construct scientific and technological basis for geological disposal of High-level Radioactive Waste (HLW). The MIU Project has three overlapping phases: Surface-based Investigation phase (Phase I), Construction phase (Phase II), and Operation phase (Phase III). The MIU Project has been ongoing the Phase II and the Phase III in 2011 fiscal year. This report shows the results of the investigation, construction and collaboration studies in fiscal year 2011, as a part of the Phase II and Phase III based on the MIU Master Plan updated in 2010.

Mizunami Underground Research Laboratory Project, Plan for fiscal year 2012

Kunimaru, Takanori; Mikake, Shinichiro; Nishio, Kazuhisa; Tsuruta, Tadahiko; Matsuoka, Toshiyuki; Ishibashi, Masayuki; Kuboshima, Koji; Takeuchi, Ryuji; Mizuno, Takashi; Sato, Toshinori; et al.

JAEA-Review 2012-028, 31 Pages, 2012/08

JAEA-Review-2012-028.pdf:3.86MB

Japan Atomic Energy Agency (JAEA) at Tono Geoscience Center (TGC) is pursuing a geoscientific research and development project namely the Mizunami Underground Research Laboratory (MIU) project in crystalline rock environment in order to construct scientific and technological basis for geological disposal of High-level Radioactive Waste (HLW). The MIU project is planned in three overlapping phases; Surface-based Investigation Phase (Phase I), Construction Phase (Phase II) and Operation Phase (Phase III). Currently, the project is under the Construction Phase and the Operation Phase. This document introduces the research and development activities planned for 2012 fiscal year based on the MIU Master Plan updated in 2010, construction plan and research collaboration plan, etc.

Direct evidence of generation and accumulation of -sheet-rich prion protein in scrapie-infected neuroblastoma cells with human IgG1 antibody specific for -form prion protein

Kubota, Toshiya*; Hamazoe, Yuta*; Hashiguchi, Shuhei*; Ishibashi, Daisuke*; Akasaka, Kazuyuki*; Nishida, Noriyuki*; Katamine, Shigeru*; Sakaguchi, Suehiro*; Kuroki, Ryota; Nakashima, Toshihiro*; et al.

Journal of Biological Chemistry, 287(17), p.14023 - 14039, 2012/04

https://doi.org/10.1074/jbc.M111.318352

We prepared -sheet-rich recombinant full-length prion protein (-form PrP) (Jackson, G. S., Hosszu, L. L., Power, A., Hill, A. F., Kenney, J., Saibil, H., Craven, C. J., Waltho, J. P., Clarke, A. R., and Collinge, J. (1999) Science 283, 1935-1937). Using this -form PrP and a human single chain Fv-displaying phage library, we have established a human IgG1 antibody specific to -form but not -form PrP, PRB7 IgG. When prion-infected ScN2a cells were cultured with PRB7 IgG, they generated and accumulated PRB7-binding granules in the cytoplasm with time, consequently becoming apoptotic cells bearing very large PRB7-bound aggregates. The SAF32 antibody recognizing the N-terminal octarepeat region of full-length PrP stained distinct granules in these cells as determined by confocal laser microscopy observation. When the accumulation of proteinase K-resistant PrP was examined in prion-infected ScN2a cells cultured in the presence of PRB7 IgG or SAF32, it was strongly inhibited by SAF32 but not at all by PRB7 IgG. Thus, we demonstrated direct evidence of the generation and accumulation of -sheet-rich PrP in ScN2a cells de novo. These results suggest first that PRB7-bound PrP is not responsible for the accumulation of -form PrP aggregates, which are rather an end product resulting in the triggering of apoptotic cell death, and second that SAF32-bound PrP lacking the PRB7-recognizing -form may represent so-called PrPSc with prion propagation activity. PRB7 is the first human antibody specific to -form PrP and has become a powerful tool for the characterization of the biochemical nature of prion and its pathology.

Residue 134 determines the dimer-tetramer assembly of nucleoside diphosphate kinase from moderately halophilic bacteria

Tokunaga, Hiroko*; Ishibashi, Matsujiro*; Arisaka, Fimio*; Arai, Shigeki; Kuroki, Ryota; Arakawa, Tsutomu*; Tokunaga, Masao*

FEBS Letters, 582(7), p.1049 - 1054, 2008/04

https://doi.org/10.1016/j.febslet.2008.02.054

nucleoside diphosphate kinase (HaNDK) forms a dimeric assembly and NDK (PaNDK) forms a tetrameric assembly. The mutation of Glu134 to Ala in HaNDK resulted in conversion of the native dimeric structure to the tetramer assembly. Conversely, the mutation of Ala134 to Glu in PaNDK leads to conversion from tetramer to dimer assembly, indicating that a single amino acid substitution at position 134 results in an alteration of the oligomeric structure of NDK. Modeling structure of HaNDK and PaNDK, based on the crystal structure of NDK, suggested sufficient repulsion by Glu134 to disrupt dimer-dimer interaction to form tetramer.

Crystallization of a 2:2 complex of Granulocyte-Colony Stimulating Factor (GCSF) with the ligand-binding region of the GCSF receptor

Honjo, Eijiro; Tamada, Taro; Maeda, Yoshitake*; Koshiba, Takumi*; Matsukura, Yasuko*; Okamoto, Tomoyuki*; Ishibashi, Matsujiro*; Tokunaga, Masao*; Kuroki, Ryota

Acta Crystallographica Section F, 61(8), p.788 - 790, 2005/08

https://doi.org/10.1107/S1744309105023080

Granulocyte colony-stimulating factor (GCSF) receptor receives signals for regulating the proliferation and differentiation of the precursor cells of granulocytes. The complex composed of two GCSFs and two GCSF receptors was crystallized. The crystal of the complex was grown in 1.0 M sodium formate and 0.1 M sodium acetate (pH4.6). It belongs to the space group 422 (or its enantiomorph 422) with unit cell dimensions of = = 110.1 , = 331.8 . However, the diffraction data from the crystal beyond 5 resolution could not be collected. Since the heterogeneity of GCSF receptor seems to interrupt growth of good quality crystals, the GCSF receptor was fractionated by achromatography. Crystals of GCSF/fractionated GCSF receptor complex were grown as a new crystal form in 0.2 M ammonium phosphate. The new crystal diffracts beyond 3.0 resolution and belongs to space group 321 (or its enantiomorph 321) with unit-cell parameters = = 134.8, = 105.7 .

Homodimeric crossover structure of the human GCSF-receptor signaling complex

Tamada, Taro; Honjo, Eijiro; Maeda, Yoshitake*; Okamoto, Tomoyuki*; Ishibashi, Matsujiro*; Tokunaga, Masao*; Kuroki, Ryota

no journal, , 

We have succeeded in crystallization of 2:2 complex between human granulocyte colony-stimulating factor (hGCSF) and the Ig-like and CRH domains of human GCSF-R (hGCSF-R) and determined its tertiary structure by X-ray crystallography at 2.8 resolution. The signaling 2:2 complex is formed via cross-over interactions between the Ig-like domain of hGCSF-R and the neighboring hGCSF, forming a two-fold axis of crystallographic symmetry. This conformation is quite different from that of the heterogeneous mGCSF-R complex, and more closely resembles the 2:2:2 active assembly of human interleukin-6 (IL-6), human IL-6 -receptor and human gp130 (which is a shared signal transducing receptor for several cytokines), and the 2:2 assembly of viral IL-6 and human gp130. The Ig-like domain cross-over structure necessary for GCSF-R activation is consistent with previously reported thermodynamic and mutational analyses.

X-ray crystallographic analysis of -Lactamase derived from sp.560

Arai, Shigeki; Tokunaga, Hiroko*; Tamada, Taro; Yonezawa, Yasushi; Adachi, Motoyasu; Yamada, Mitsugu; Ishibashi, Matsujiro*; Tokunaga, Masao*; Kuroki, Ryota

no journal, , 

Halophilic proteins can bind various inorganic ions with its negative charges located over the molecular surface. We are investigating the molecular structure of the halophilic proteins because halophilic proteins might be used as a material capturing for the rare metals and/or the radioactive metal ions. Recently, we succeeded in X-ray crystallographic analysis of the halophilic -Lactamase (HaBLA) derived from sp.560 at 3.0 resolution. From this structural analysis, we found that the back bone structure and the positively charged active site feature of HaBLA was similar to those of non-halophilic BLA. The molecular surface of HaBLA were, however, occupied by large number of negative charges. This structural information is very useful to improve the specificity of metals such as Cs or Sr.