A03-2 石森 浩一郎（北海道大学大学院 理学研究院）

A03-2 石森 浩一郎（北海道大学大学院 理学研究院）

  1. T. Uchida, N. Dojun, Y. Sekine, K. Ishimori: “Role of His63 in HutZ from Vibrio cholerae in the Heme Degradation Reaction and Heme Binding” Dalton Trans. 48, 5408-5416 (2019) DOI: https://doi.org/10.1039/c9dt00926d
  2. S. Konno, K. Doi, K. Ishimori: “Uncovering Dehydration in Cytochrome c Refolding from Urea- and Guanidine Hydrochloride-denatured Unfolded State by High Pressure Spectroscopy” Biophys. Physicobiol. 16, 18 – 27 (2019) DOI: https://doi.org/10.2142/biophysico.16.0_18
  3. Y. Nishitani, H. Okutani, Y. Takeda, T. Uchida, K. Iwai, K. Ishimori: “Specific Heme Binding to Heme Regulatory Motifs in Iron Regulatory Proteins and Its Functional Significance” J. Inorg. Biochem. 198, 110726 (2019) DOI: https://doi.org/10.1016/j.jinorgbio.2019.110726
  4. 【領域内連携】N. Muraki, C. Kitatsuji, Y. Okamoto, T. Uchida, K. Ishimori, S. Aono: “Structural Basis for the Heme Transfer Reaction in Heme Uptake Machinery from Corynebacteria” Chem. Commun. (Camb.) 55, 13862-13867 (2019) DOI: https://doi.org/10.1039/c9cc07369h
  5. T. Uchida, N. Dojun, K. Ota, Y. Sekine, Y. Nakamura, S. Umetsu, K. Ishimori: “Role of Conserved Arginine in the Heme Distal Site of HutZ from Vibrio cholerae in the Heme Degradation Reaction” Arch. Biochem. Biophys. 677, 108165 (2019) DOI: https://doi.org/10.1016/j.abb.2019.108165
  6. N. Dojun, K. Muranishi, K. Ishimori, T. Uchida: “A Single Mutation Converts Alr5027 from Cyanobacteria Nostoc sp. PCC 7120 to a Heme-binding Protein with Heme-degrading Ability” J. Inorg. Biochem. 203, 110916 (2020) DOI: https://doi.org/10.1016/j.jinorgbio.2019.110916
  7. T. Uchida, N. Dojun, K. Muranishi, K. Ishimori: “A Single Mutation Converts Alr5027 from Cyanobacteria Nostoc sp. PCC 7120 to a Heme-Binding Protein with Heme-Degrading Ability” J. Inorg. Biochem. 203, 110916 (2020) DOI: https://doi.org/10.1016/j.jinorgbio.2019.110916
  8. W. Sato, S. Hitaoka, T. Uchida, K. Shinzawa-Itoh, K. Yoshizawa, S. Yoshikawa, K. Ishimori: “Osmotic Pressure Effects Identify Dehydration upon Cytochrome c – Cytochrome c Oxidase Complex Formation Contributing to a Specific Electron Pathway Formation” Biochem. J., 477, 1565-1578 (2020) DOI: https://doi.org/10.1042/BCJ20200023
  9. Yamamoto, T. Tsukamoto, K. Suzuki, E. Hashimoto, Y. Kobashigawa, K. Shibasaki, T. Uchida, F. Inagaki, M. Demura, K. Ishimori: “Spectroscopic Characterization of Halorhodopsin Reconstituted into Nanodiscs Using Native Lipids” Biophys. J. 118, 2853-2865 (2020) DOI: https://doi.org/10.1016/j.bpj.2020.04.021
  10. D. Nam, M. Matsumoto, T. Uchida, M. R. O’Brian, K. Ishimori: “Mechanistic Insights into Heme-mediated Transcriptional Regulation via a Bacterial Manganese-binding Iron Regulator, Iron Response Regulator (Irr)” J. Biol. Chem., 295, 11316-11325 (2020) DOI: https://doi.org/10.1074/jbc.RA119.011855
  11. T. Uchida, I. Omura, S. Umetsu, K. Ishimori: “Radical Transfer But Not Heme Distal Residues is Essential for pH Dependence of Dye-decolorizing Activity of Peroxidase from Vibrio cholerae” J. Inorg. Biochem. 219, 111422 (2021) DOI: https://doi.org/10.1016/j.jinorgbio.2021.111422
  12. T. Saio, S. Hiramatsu, M. Asada, H. Nakagawa, K. Shimizu, H. Kumeta, T. Nakamura, K. Ishimori: “Conformational Ensemble of a Multidomain Protein Explored by Gd3+ Electron Pparamagnetic Resonance” Biophys. J. 120, 2943-2951 (2021) DOI: https://doi.org/10.1016/j.bpj.2021.06.033
  13. H. Zhu, M. Matsusaki, T. Sugawara, K. Ishimori, T. Saio: “Zinc-Dependent Oligomerization of Thermus thermophilus Trigger Factor Chaperone” Biology, 10, 1106 (2021) DOI: https://doi.org/10.3390/biology10111106
  14. K. Rizzolo, A. Y. H. Yu, A. Ologbenla, S. -R. Kim, H. Zhu, K. Ishimori, G. Thibault, E. Leung, Y. W. Zhang, M. Teng, N. Haniszewski, N. Miah, S. Phanse, Z. Minic, S. Lee, J. D. Caballero, M. Babu, F. T. F. Tsai, T. Saio, W. A. Houry: “Functional Cooperativity between the Trigger Factor Chaperone and the ClpXP Proteolytic Complex” Nat. Commun., 12, 281 (2021) DOI: https://doi.org/1038/s41467-020-20553-x
  15. K. Muranishi, K. Ishimori, T. Uchida: “Regulation of the Expression of the Nickel Uptake System in Vibrio cholerae by Iron and Heme via Ferric Uptake regulator (Fur)” J. Inorg. Biochem. 228, 111713 (2022) DOI: https://doi.org/10.1016/j.jinorgbio.2022.111713
  16. T. Uchida, K. Ota, A. Tatsumi, S. Takeuchi, K. Ishimori: “Metal Sensing by a Glycine–Histidine Repeat Sequence Regulates the Heme Degradation Activity of PM0042 from Pasteurella multocida” Inorg. Chem., 61, 13543–13553 (2022) DOI: https://doi.org/10.1021/acs.inorgchem.2c02172
  17. I. Omura, K. Ishimori, T. Uchida: “Converting Cytochrome c into a DyP-like Metalloenzyme” Dalton Trans. 51, 12641-12649 (2022) DOI: https://doi.org/10.1039/D2DT02137D
  18. D. Nam, W. Motegi, K. Ishimori, T. Uchida: “Heme Binding to Cold Shock Protein D, CspD, from Vibrio cholerae” Biochem. Biophys. Res. Commun., 624, 151-156 (2022) DOI: https://doi.org/10.1016/j.bbrc.2022.07.074
  19. K. Kawagoe, M. Kumashiro, T. Mabuchi, H. Kumeta, K. Ishimori, T. Saio: “Heat-Induced Conformational Transition Mechanism of Heat Shock Factor 1 Investigated by Tryptophan Probe” Biochemistry, 61, 2897–290 (2022) DOI: https://doi.org/10.1021/acs.biochem.2c00492
  20. Z. Du, E. Nam, Y. Lin, M. Hong, T. Molnár, I. Kondo, K. Ishimori, M.-H. Baik, Y.-H. Lee, M. H. Lim: “Unveiling the impact of oxidation-driven endogenous protein interactions on the dynamics of amyloid-β aggregation and toxicity” Chem. Sci., 14, 5340–5349 (2023) DOI: https://doi.org/10.1039/D3SC00881A
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