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物質創成科学研究科 / Graduate School of Materials Science

物質創成科学研究科 / Graduate School of Materials Science

 

Recent Submissions

  • Nonoguchi, Yoshiyuki; Nakano, Motohiro; Murayama, Tomoko; Hagino, Harutoshi; Hama, Shota; Miyazaki, Koji; Matsubara, Ryosuke; Nakamura, Masakazu; Kawai, Tsuyoshi (John Wiley and Sons, 2016-04-25)
    After more than three decades of molecular and carbon-based electronics, the creation of air- and thermally stable n-type materials remains a challenge in the development of future p/n junction devices such as solar cells ...
  • Taguchi, M.; Chainani, A.; Ueda, S.; Matsunami, M.; Ishida, Y.; Eguchi, R.; Tsuda, S.; Takata, Y.; Yabashi, M.; Tamasaku, K.; Nishino, Y.; Ishikawa, T.; Daimon, H.; Todo, S.; Tanaka, H.; Oura, M.; Senba, Y.; Ohashi, H.; Shin, S. (American Physical Society, 2015-12-17)
    We study the electronic structure of bulk single crystals and epitaxial films of Fe3O4. Fe 2p core level spectra show clear differences between hard x-ray (HAX) and soft x-ray photoemission spectroscopy (PES). The ...
  • Fujii, Mami N.; Ishikawa, Yasuaki; Miwa, Kazumoto; Okada, Hiromi; Uraoka, Yukiharu; Ono, Shimpei (Macmillan Publishers, 2015-12-18)
    The use of indium-gallium-zinc oxide (IGZO) has paved the way for high-resolution uniform displays or integrated circuits with transparent and flexible devices. However, achieving highly reliable devices that use IGZO for ...
  • Yamanaka, Masaru; Nagao, Satoshi; Komori, Hirofumi; Higuchi, Yoshiki; Hirota, Shun (John Wiley & Sons, Ltd, 2015-03-01)
    Cytochrome c555 from hyperthermophilic bacteria Aquifex aeolicus (AA cyt c555) is a hyperstable protein belonging to the cyt c protein family, which possesses a unique long 310-α-310 helix containing the heme-ligating ...
  • Nagao, Satoshi; Ishikawa, Haruto; Yamada, Takuya; Mizutani, Yasuhisa; Hirota, Shun (Springer Berlin Heidelberg, 2015-04-01)
    Myoglobin (Mb) is a monomeric oxygen storage hemoprotein, and has been shown to form a domain-swapped dimer. In this study, monomeric and dimeric carbon monoxide (CO)-bound Mb (MbCO) exhibited similar absorption spectra. ...
  • Wang, Zhonghua; Matsuo, Takashi; Nagao, Satoshi; Hirota, Shun (The Royal Society of Chemistry, 2011-04-12)
    The peroxidase activity of horse cytochrome c was enhanced by its dimerization, where its Compound III (oxy-form) and Compound I (oxoferryl porphyrin [small pi]-cation radical) species were detected in the reactions with ...
  • Takahashi, Isao; Kuroiwa, Shigeki; Lindfors, Hanna E.; Ndamba, Lionel A.; Hiruma, Yoshitaka; Yajima, Tatsuo; Okishio, Nobuyuki; Ubbink, Marcellus; Hirota, Shun (John Wiley & Sons, Ltd., 2009-04-20)
    To photomodulate the interaction of the phosphatidylinositol 3-kinase SH3 domain with a peptide ligand, a cyclic peptide (cyclic-1) with a photolabile side chain-to-side chain linker was synthesized. The conformation of ...
  • Nugraheni, AriDwi; Nagao, Satoshi; Yanagisawa, Sachiko; Ogura, Takashi; Hirota, Shun (Springer Berlin Heidelberg, 2013-03-01)
    We have previously shown that methionine-heme iron coordination is perturbed in domain-swapped dimeric horse cytochrome c. To gain insight into the effect of methionine dissociation in dimeric cytochrome c, we investigated ...
  • Hirota, Shun; Kawahara, Takumi; Beltramini, Mariano; Di Muro, Paolo; Magliozzo, Richard S.; Peisach, Jack; Powers, Linda S.; Tanaka, Naoki; Nagao, Satoshi; Bubacco, Luigi (The American Society for Biochemistry and Molecular Biology, Inc., 2008-11-14)
    Flash photolysis and K-edge x-ray absorption spectroscopy (XAS) were used to investigate the functional and structural effects of pH on the oxygen affinity of three homologous arthropod hemocyanins (Hcs). Flash photolysis ...
  • Wang, Zhonghua; Ando, Yuki; Nugraheni, Ari Dwi; Ren, Chunguang; Nagao, Satoshi; Hirota, Shun (The Royal Society of Chemistry, 2014-09-01)
    Met80 of cytochrome c (cyt c) has been shown to dissociate from its heme iron when cyt c interacts with cardiolipin (CL), which triggers the release of cyt c into the cytosol initiating apoptosis. We found that the mass ...
  • Hirota, Shun; Hattori, Yoko; Nagao, Satoshi; Taketa, Midori; Komori, Hirofumi; Kamikubo, Hironari; Wang, Zhonghua; Takahashi, Isao; Negi, Shigeru; Sugiura, Yukio; Kataoka, Mikio; Higuchi, Yoshiki (National Academy of Sciences., 2010-07-20)
    Cytochrome c (cyt c) is a stable protein that functions in a monomeric state as an electron donor for cytochrome c oxidase. It is also released to the cytosol when permeabilization of the mitochondrial outer membrane occurs ...
  • Hirota, Shun; Tanaka, Naoki; Mičetić, Ivan; Di Muro, Paolo; Nagao, Satoshi; Kitagishi, Hiroaki; Kano, Koji; Magliozzo, Richard S.; Peisach, Jack; Beltramini, Mariano; Bubacco, Luigi (The American Society for Biochemistry and Molecular Biology, Inc., 2010-06-18)
    Hemocyanin (Hc) is an oxygen carrier protein in which oxygen binding is regulated by allosteric effectors such as H+ and l-lactate. Isothermal titration calorimetric measurements showed that l-lactate binds to dodecameric ...
  • Nagao, Satoshi; Osuka, Hisao; Yamada, Takuya; Uni, Takeshi; Shomura, Yasuhito; Imai, Kiyohiro; Higuchi, Yoshiki; Hirota, Shun (The Royal Society of Chemistry, 2012-07-24)
    Myoglobin (Mb) stores dioxygen in muscles, and is a fundamental model protein widely used in molecular design. The presence of dimeric Mb has been known for more than forty years, but its structural and oxygen binding ...
  • Nagao, Satoshi; Asami, Osamu; Yasui, Hiroyuki; Hirota, Shun (Elsevier, 2011-01-21)
    Human myoglobin (hMb) possesses a cysteine (Cys) residue which is rare among mammalian Mbs. To investigate the effects of this unique Cys residue at the amino acid position 110 (Cys110) on hMb reactions, we studied the ...
  • Hirota, Shun; Suzuki, Masako; Watanabe, Yoshihito (Elsevier, 2004-01-05)
    Effect of a hydrophobic peptide on folding of oxidized cytochrome c (cyt c) is studied with trityrosine. Folding of cyt c was initiated by pH jump from 2.3 (acid-unfolded) to 4.2 (folded). The Soret band of the 2-ms transient ...
  • Osuka, Hisao; Shomura, Yasuhito; Komori, Hirofumi; Shibata, Naoki; Nagao, Satoshi; Higuchi, Yoshiki; Hirota, Shun (Elsevier, 2013-01-04)
    [NiFe] hydrogenase catalyzes reversible oxidation of molecular hydrogen. Its active site is constructed of a hetero dinuclear Ni-Fe complex, and the oxidation state of the Ni ion changes according to the redox state of the ...
  • Tai, Hulin; Nishikawa, Koji; Suzuki, Masayuki; Higuchi, Yoshiki; Hirota, Shun (WILEY-VCH Verlag, 2014-10-08)
    [NiFe] hydrogenase catalyzes the reversible cleavage of H2. The electrons produced by the H2 cleavage pass through three Fe-S clusters in [NiFe] hydrogenase to its redox partner. It has been reported that the Ni-SIa, Ni-C, ...
  • Nagao, Satoshi; Ueda, Mariko; Osuka, Hisao; Komori, Hirofumi; Kamikubo, Hironari; Kataoka, Mikio; Higuchi, Yoshiki; Hirota, Shun (Public Library of Science, 2015-04-08)
    Cytochrome c (cyt c) family proteins, such as horse cyt c, Pseudomonas aeruginosa cytochrome c551 (PA cyt c551), and Hydrogenobacter thermophilus cytochrome c552 (HT cyt c552), have been used as model proteins to study the ...
  • Takahashi, Isao; Honda, Yuichiro; Hirota, Shun (WILEY-VCH Verlag, 2009-07-11)
    Self-assembled monolayers (SAMs) of both trans- and cis-azobenzene ligands can bind CuII ions. Ions bound to the trans ligand are released by cyclic voltammetry (CV) redox scans whereas those bound to the cis ligand are ...
  • Deshpande, Megha Subhash; Junedi, Sendy; Prakash, Halan; Nagao, Satoshi; Yamanaka, Masaru; Hirota, Shun (The Royal Society of Chemistry, 2014-10-10)
    Double stranded DNA was cleaved oxidatively by incubation with oxygenated myoglobin, and Lys96Cys sperm whale myoglobin in its stable ferric form functioned as an artificial nuclease under air by formation of an oxygenated ...

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