Hagiwara Lab, Department of Biochemistry and Applied Chemistry, National Institute of Technology, Kurume College

久留米高専 生物応用化学科 萩原研究室

Publications

研究業績

【原著論文】

  1. Regulating the protonation state of biliverdin and catalytic glutamate residue via single-residue mutation of phycocyanobilin:ferredoxin oxidoreductase following neutron crystallography,
    Joutsuka T., Nanasawa R., Igarashi K., Horie K., Sugishima M., Hagiwara Y., Wada K., Fukuyama K., Yano N., Mori S., Ostermann A., Kusaka K., Unno M.,
    Journal of Biological Chemistry, 299, 102763 (2023).

  2. Amphiphilic triphenylamine-benzothiadiazole dyes: preparation, fluorescence and aggregation behavior, and enzyme fluorescence detection,
    Ishi-I T., Kawai K., Shirai Y., Kitahara I., Hagiwara Y.,
    Photochemical and Photobiological Sciences, 18, 1447-1460 (2019).

  3. Crystal Growth of a Bilin Reductase PcyA I86D Mutant-Substrate Complex for Neutron Crystallography,
    Igarashi K., Hagiwara Y., Sugishima M., Wada K., Fukuyama K., Ikeda A., Yano N., Kusaka K., Ostermann A., Unno M.,
    Crystal Growth and Design, 18, 5174-5181 (2018).

  4. A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity,
    Takao H., Hirabayashi K., Nishigaya Y., Kouriki H., Nakaniwa T., Hagiwara Y., Harada J., Sato H., Yamazaki T., Sakakibara Y., Suiko M., Asada Y., Takahashi Y., Yamamoto K., Fukuyama K., Sugishima M., Wada K.,
    Nature Communications, 8, 14397 (2017).

  5. Atomic-resolution structure of the phycocyanobilin:ferredoxin oxidoreductase I86D mutant in complex with fully protonated biliverdin,
    Hagiwara Y., Wada K., Irikawa T., Sato H., Yamamoto K., Fukuyama K., Sugishima M.,
    FEBS Letters, 590, 3425-3434 (2016).

  6. Insights into the Proton Transfer Mechanism of a Bilin Reductase PcyA Following Neutron Crystallography,
    Unno M., Ishikawa-Suto K., Kusaka K., Tamada T., Hagiwara Y., Sugishima M., Wada K., Yamada T., Tomoyori K., Hosoya T., Tanaka I., Niimura N., Kuroki R., Inaka K., Ishihara M., Fukuyama K.,
    J. Am. Chem. Soc., 137, 5452-5460 (2015).

  7. Inactivation of the conserved open reading frame ycf34 of Synechocystis sp. PCC 6803 interferes with the photosynthetic electron transport chain,
    Wallner T., Hagiwara Y., Bernat G., Sobotka R., Reijerse J. E., Frankenberg-Dinkel N. and Wilde A.,
    Biochimica et Biophysica Acta - Bioenergetics, 1817, 2016-2026 (2012).

  8. Expression, crystallization and X-ray data collection of the cyanobacterial biliverdin reductase,
    Watanabe A., Hirata K., Hagiwara Y., Yutani Y., Sugishima M., Yamamoto M., Fukuyama K. and Wada K.,
    Acta Crystallogr. Sect. F, 67, 313-317 (2011).

  9. One residue substitution in PcyA leads to unexpected changes in tetrapyrrole substrate binding,
    Wada K., Hagiwara Y., Yutani Y. and Fukuyama K.,
    Biochem. Biophys. Res. Commun., 402, 373-377 (2010).

  10. Structural insights into vinyl reduction regiospecificity of phycocyanobilin:ferredoxin oxidoreductase (PcyA),
    Hagiwara Y., Sugishima M., Khawn H., Kinoshita H., Inomata K., Shang L., Lagarias J. C., Takahashi Y. and Fukuyama K.,
    J. Biol. Chem., 285, 1000-1007 (2010).
      -> selected as a "Papers of the Week".
      -> selected as a "Must Read", Faculty of 1000.

  11. Induced-fitting and electrostatic potential change of PcyA upon substrate binding demonstrated by the crystal structure of the substrate-free form,
    Hagiwara Y., Sugishima M., Takahashi Y. and Fukuyama K.,
    FEBS Letters, 580, 3823-3828 (2006).

  12. Crystal structure of phycocyanobilin:ferredoxin oxidoreductase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phycocyanobilin,
    Hagiwara Y.*, Sugishima M.*, Takahashi Y. and Fukuyama K.,
    Proc. Natl. Acad. Sci. U.S.A., 103, 27-32 (2006).
      -> selected as "From the Cover".
      * These authors contributed equally to this work.

  13. Crystal structure of dimeric heme oxygenase-2 from Synechocystis sp. PCC 6803 in complex with heme,
    Sugishima M., Hagiwara Y., Zhang X., Yoshida T., Migita C. T. and Fukuyama K.,
    Biochemistry, 44, 4257-4266 (2005).

【総説】

  1. ビリン還元酵素PcyAと基質ビリベルジン複合体の中性子結晶構造解析で見えてきたもの、
    海野昌喜, 日下勝弘, 玉田太郎, 杉島正一, 和田啓, 萩原義徳, 福山恵一、
    波紋、26, 130-134 (2016).

  2. 中性子結晶構造解析で明らかになったビリン還元酵素PcyA基質複合体の二つの水素化状態と構造的特徴、
    海野昌喜、杉島正一、和田啓、萩原義徳、日下勝弘、玉田太郎、福山恵一、
    日本結晶学会誌、57, 297-303 (2015).

  3. フェレドキシン依存性ビリン還元酵素の構造研究、
    杉島正一、萩原義徳、高橋康弘、福山恵一、
    日本結晶学会誌、48, 283-289 (2006).

【招待講演】

  1. シアノバクテリアの光捕集と光受容に関わるタンパク質の構造と機能、
    萩原 義徳
    日本地衣学会第14回大会 一般公開シンポジウム
    福岡、2015年7月

  2. フェレドキシン依存性ビリン還元酵素PcyAによる光受容色素合成の構造生物学、
    萩原 義徳
    第87回日本生化学会大会 フォーラム「ヘム・ビリン代謝の生化学と構造生物学」
    京都、2014年10月

  3. Scientific and Scenic life in Germany,
    Hagiwara Y.,
    Symposium on EU-Japan Collaboration in Education, Research and Exchanges,
    Brussels, Belgium, Dec. 2011.



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