研究業績
  • Diffusion-limited biosensing of dissolved oxygen by direct electron transfer-type bioelectrocatalysis of multi-copper oxidases immobilized on porous gold microelectrodes
    Miyata M., Kitazumi Y., Shirai O., Kataoka K., Kano K.
    Journal of Electroanalytical Chemistry., 860, (2020)
    10.1016/j.jelechem.2020.113895

  • Roles of the indole ring of Trp396 covalently bound with the imidazole ring of His398 coordinated to type I copper in bilirubin oxidase
    Kataoka K., Ito T., Okuda Y., Sakai Y., Yamashita S., Sakurai T.
    Biochemical and Biophysical Research Communications., 521, 620-624 (2020)
    10.1016/j.bbrc.2019.10.159

  • A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity
    Waki T., Mameda R., Nakano T., Yamada S., Terashita M., Ito K., Tenma N., Li Y., Fujino N., Uno K., Yamashita S., Aoki Y., Denessiouk K., Kawai Y., Sugawara S., Saito K., Yonekura-Sakakibara K., Morita Y., Hoshino A., Takahashi S., Nakayama T.
    Nature Communications., 11(2020)
    10.1038/s41467-020-14558-9

  • Kinetic and structural insight into a role of the re-face Tyr328 residue of the homodimer type ferredoxin-NADP+ oxidoreductase from Rhodopseudomonas palustris in the reaction with NADP+/NADPH
    Seo D., Muraki N., Kurisu G.
    Biochimica et Biophysica Acta - Bioenergetics., 1861 (2020)
    10.1016/j.bbabio.2019.148140

  • A bio-solar cell with thylakoid membranes and bilirubin oxidase
    Adachi T., Kataoka K., Kitazumi Y., Shirai O., Kano K.
    Chemistry Letters., 48, 686-689 (2019)
    10.1246/cl.190176

  • Structural changes of the trinuclear copper center in bilirubin oxidase upon reduction
    Tokiwa T., Shoji M., Sladek V., Shibata N., Higuchi Y., Kataoka K., Sakurai T., Shigeta Y., Misaizu F.
    Molecules., 24(2019)
    10.3390/molecules24010076

  • Redox Potential-Dependent Formation of an Unusual His–Trp Bond in Bilirubin Oxidase
    Akter M., Tokiwa T., Shoji M., Nishikawa K., Shigeta Y., Sakurai T., Higuchi Y., Kataoka K., Shibata N.
    Chemistry - A European Journal., 24, 18052-18058 (2018)
    10.1002/chem.201803798

  • Physical interactions among flavonoid enzymes in snapdragon and torenia reveal the diversity in the flavonoid metabolon organization of different plant species
    Fujino N., Tenma N., Waki T., Ito K., Komatsuzaki Y., Sugiyama K., Yamazaki T., Yoshida S., Hatayama M., Yamashita S., Tanaka Y., Motohashi R., Denessiouk K., Takahashi S., Nakayama T.
    Plant Journal., 94, 372-392 (2018)
    10.1111/tpj.13864

  • Purification and characterization of small and large rubber particles from Hevea brasiliensis
    Yamashita S., Mizuno M., Hayashi H., Yamaguchi H., Miyagi-Inoue Y., Fushihara K., Koyama T., Nakayama T., Takahashi S.
    Bioscience, Biotechnology and Biochemistry., 82, 1011-1020 (2018)
    10.1080/09168451.2017.1401913

  • Identification and characterization of a novel bacterial β-glucosidase that is highly specific for the β-1,2-glucosidic linkage of sesaminol triglucoside
    Sakurai A., Hongo S., Nair A., Waki T., Oikawa D., Nishio T., Shimoyama T., Takahashi S., Yamashita S., Nakayama T.
    Bioscience, Biotechnology and Biochemistry., 82, 1518-1521 (2018)
    10.1080/09168451.2018.1476123

  • C-terminal residues of ferredoxin-NAD(P)+ reductase from Chlorobaculum tepidum are responsible for reaction dynamics in the hydride transfer and redox equilibria with NADP+/NADPH
    Seo D., Asano T.
    Photosynthesis Research., 136, 275-290 (2018)
    10.1007/s11120-017-0462-z

  • Amino acids located in the outer-sphere of the trinuclear copper center in a multicopper oxidase, CueO as the putative electron donor in the four-electron reduction of dioxygen
    Sakurai T., Yamamoto M., Ikeno S., Kataoka K.
    Biochimica et Biophysica Acta - Proteins and Proteomics., 1865, 997-1003 (2017)
    10.1016/j.bbapap.2017.04.005

  • Heterologous expression of Halomonas halodenitrificans nitric oxide reductase and its N-terminally truncated NorC subunit in Escherichia coli
    Sakurai N., Kataoka K., Sugaya N., Shimodaira T., Iwamoto M., Shoda M., Horiuchi H., Kiyono M., Ohta Y., Triwiyono B., Seo D., Sakurai T.
    Journal of Inorganic Biochemistry., 169, 61-67 (2017)
    10.1016/j.jinorgbio.2017.01.006

  • Alpha/beta-hydrolases: A unique structural motif coordinates catalytic acid residue in 40 protein fold families
    Dimitriou P.S., Denesyuk A., Takahashi S., Yamashita S., Johnson M.S., Nakayama T., Denessiouk K.
    Proteins: Structure, Function and Bioinformatics., 85, 1845-1855 (2017)
    10.1002/prot.25338

  • Toward total elucidation of biosynthetic mechanism of natural rubber
    Takahashi S., Yamashita S., Fushihara K.
    Kobunshi., 66, 278-280 (2017)

  • Biochemical, spectroscopic and X-ray structural analysis of deuterated multicopper oxidase CueO prepared from a new expression construct for neutron crystallography
    Akter M., Inoue C., Komori H., Matsuda N., Sakurai T., Kataoka K., Higuchi Y., Shibata N.
    Acta Crystallographica Section:F Structural Biology Communications., 72, 788-794 (2016)
    10.1107/S2053230X1601400X

  • Exogenous acetate ion reaches the type II copper centre in CueO through the water-excretion channel and potentially affects the enzymatic activity
    Komori H., Kataoka K., Tanaka S., Matsuda N., Higuchi Y., Sakurai T.
    Acta Crystallographica Section:F Structural Biology Communications., 72, 558-563 (2016)
    10.1107/S2053230X16009237

  • Identification and reconstitution of the rubber biosynthetic machinery on rubber particles from Hevea brasiliensis
    Yamashita S., Yamaguchi H., Waki T., Aoki Y., Mizuno M., Yanbe F., Ishii T., Funaki A., Tozawa Y., Miyagi-Inoue Y., Fushihara K., Nakayama T., Takahashi S.
    eLife., 5, 0-0 (2016)
    10.7554/eLife.19022.001

  • Identification of protein-protein interactions of isoflavonoid biosynthetic enzymes with 2-hydroxyisoflavanone synthase in soybean (Glycine max (L.) Merr.)
    Waki T., Yoo D., Fujino N., Mameda R., Denessiouk K., Yamashita S., Motohashi R., Akashi T., Aoki T., Ayabe S.-I., Takahashi S., Nakayama T.
    Biochemical and Biophysical Research Communications., 469, 546-551 (2016)
    10.1016/j.bbrc.2015.12.038

  • Kinetics of NADP+/NADPH reduction–oxidation catalyzed by the ferredoxin-NAD(P)+ reductase from the green sulfur bacterium Chlorobaculum tepidum
    Seo D., Kitashima M., Sakurai T., Inoue K.
    Photosynthesis Research., 130, 479-489 (2016)
    10.1007/s11120-016-0285-3

  • Pre-steady-state kinetic studies of redox reactions catalysed by Bacillus subtilis ferredoxin-NADP+ oxidoreductase with NADP+/NADPH and ferredoxin
    Seo D., Soeta T., Sakurai H., Sétif P., Sakurai T.
    Biochimica et Biophysica Acta - Bioenergetics., 1857, 678-687 (2016)
    10.1016/j.bbabio.2016.03.005

  • A pirin-like protein from Pseudomonas stutzeri and its quercetinase activity
    Widiatningrum T., Maeda S., Kataoka K., Sakurai T.
    Biochemistry and Biophysics Reports., 3, 144-149 (2015)
    10.1016/j.bbrep.2015.08.001

  • A novel resting form of the trinuclear copper center in the double mutant of a multicopper oxidase, CueO, Cys500Ser/Glu506Ala
    Kajikawa T., Sugiyama R., Kataoka K., Sakurai T.
    Journal of Inorganic Biochemistry., 149, 88-90 (2015)
    10.1016/j.jinorgbio.2015.03.005

  • Replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP+ oxidoreductase activity toward NADPH
    Seo D., Naito H., Nishimura E., Sakurai T.
    Photosynthesis Research., 125, 321-328 (2015)
    10.1007/s11120-015-0099-8

  • Study on Dioxygen Reduction by Mutational Modifications of the Hydrogen Bond Network Leading from Bulk Water to the Trinuclear Copper Center in Bilirubin Oxidase;
    H. Morishita, D. Kurita, K. Kataoka, and T. Sakurai,
    Biochem. Biophys. Res. Commun., 450, 767-772 (2014)
    https://doi.org/10.1016/j.bbrc.2014.06.052

  • New Insights into the Catalytic Active-Site Structure of Multicopper Oxidases;
    H. Komori, R. Sugiyama, K. Kataoka, K. Miyazaki, Y. Higuchi and T. Sakurai,
    Acta Cryst. D70, 772-779 (2014).
    https://doi.org/10.1107/S1399004713033051

  • Crystal Structure of the CueO Mutants at Glu506, the Key Amino Acid Located in the Proton Transfer Pathway for Dioxygen Reduction;
    H. Komori, T. Kajikawa, K. Kataoka, Y. Higuchi, and T. Sakurai,
    Biochem. Biophys. Res. Commun., 438, 686-690 (2013)
    https://doi.org/10.1016/j.bbrc.2013.07.121

  • Role of the Hydrogen Bond Connecting the Ligands for Substrate and Type I Copper in the Cuprous Oxidase, CueO;
    K. Kataoka and T. Sakurai,
    Chem. Lett. 42, 1102-1104 (2013)
    https://doi.org/10.1246/cl.130422

  • Modifications of Laccase Activities of Copper Efflux Oxidase, CueO by Synergistic Mutations in the First and Second Coordination Spheres of the Type I Copper Center;
    K. Kataoka, H. Kogi, S. Tsujimura, and T. Sakurai,
    Biochem. Biophys. Res. Commun., 431, 393-397 (2013)
    https://doi.org/10.1016/j.bbrc.2013.01.040

  • Electrochemical Characterization of a Unique "Neutral" Laccase from Flammulina velutipes;
    K. Saito, S. Kurose, Y. Tsujino, T. Osakai, K. Kataoka, T. Sakurai, and E. Tamiya,
    J. Biosci. Bioeng., 115, 159-167 (2013)
    https://doi.org/10.1016/j.jbiosc.2012.09.011

2012年以前ものはこちらから（→生化研旧サイト）