研究成果

• 原著論文
• 総説・解説等

原著論文

2025

• Cryo-Raman Observation on the Photocycle of a Light-Driven Cl– Pump from Mastigocladopsis repens at High Cl– Concentration
  Miyazaki, K., Kikukawa, T., Unno, M., Fujisawa, T.
  The Journal of Physical Chemistry B, 129, 3740-3746 (2025)

2024

• Chromophore Structural Change during the Photocycle of a Light-Driven Cl– Pump from Mastigocladopsis repens: A Cryogenic Raman Study
  Miyazaki, K., Kikukawa, T., Unno, M., Fujisawa, T.
  The Journal of Physical Chemistry B, 128, 9692-9698 (2024)


• A photoswitchable CENP-E inhibitor with single blue-green light to control chromosome positioning in mitotic cells
  Matsuo, K., Kikukawa, T., Waku, T., Kobori, A., Tamaoki, N.
  RSC Med. Chem., 15, 3795-3799 (2024)


• Contribution of Proteorhodopsin to Light-Dependent Biological Responses in Hymenobacter nivis P3^T Isolated from Red Snow in Antarctica
  Kondo, K., Ohtake, R., Nakano, S., Terashima, M., Kojima, H., Fukui, M., Demura, M., Kikukawa, T., Tsukamoto, T.
  Biochemistry, 63, 2257-2265 (2024)


• Direct detection of the chloride release and uptake reactions of Natronomonas pharaonis halorhodopsin
  Hamada, C., Murabe, K., Tsukamoto, T., Kikukawa, T.
  J. Biol. Chem., 300, 107712 (2024)


• Spatiotemporal regulation of CENP-E-guided chromosomes using a fast-relaxing arylazopyrazole photoswitch
  Matsuo, K., Uehara, R., Kikukawa, T., Waku, T., Kobori, A., Tamaoki, N.
  Chem Commun (Camb). 60, 6611-6614, doi: 10.1039/d4cc01922a.


• Configurational Changes of Retinal Schiff Base during Membrane Na+ Transport by a Sodium Pumping Rhodopsin
  Fujisawa, T., Kinoue, K., Seike, R., Kikukawa, T., Unno, M.
  J. Phys. Chem. Lett., 22, 1993-1998 (2024)

2023

• Multistep conformational changes leading to the gate opening of light-driven sodium pump rhodopsin
  Sato, Y., Hashimoto, T., Kato, K., Okamura, A., Hasegawa, K., Shinone, T., Tanaka, Y., Tanaka, Y., Tsukazaki, T., Tsukamoto, T., Demura, M., Yao, M., and Kikukawa, T.
  J. Biol. Chem. 299, 105393 (2023)


• The preferential transport of NO3- by full-length Guillardia theta anion channelrhodopsin 1 is enhanced by its extended cytoplasmic domain
  Ohki, Y., Shinone, T., Inoko, S., Sudo, M., Demura, M., Kikukawa, T., Tsukamoto, T.
  J. Biol. Chem. 299, 105305 (2023)


• A Basic Study of the Effects of Mulberry Leaf Administration to Healthy C57BL/6 Mice on Gut Microbiota and Metabolites
  Gan, L., Inamura, Y., Shimizu, Y., Yokoi, Y., Ohnishi, Y., Song, Z., Kumaki, Y., Kikukawa, T., Demura, M., Ito, M., Ayabe, T., Nakamura, K., Aizawa, T.
  Metabolites, 13, 1003 (2023)


• Key determinants for signaling in the sensory rhodopsin II/transducer complex are different between Halobacterium salinarum and Natronomonas pharaonis
  Matsunami-Nakamura, R., Tamogami, J., Takeguchi, M., Ishikawa, J., Kikukawa, T., Kamo, N., Nara, T.
  FEBS Lett., 597, 2334-2344 (2023)


• Antimicrobial Properties and Mode of Action of Cryptdin-4, a Mouse α-Defensin Regulated by Peptide Redox Structures and Bacterial Cultivation Conditions
  Wang Y, Song Y, Yan S, Hiramine R, Ohnishi Y, Yokoi Y, Nakamura K, Kikukawa T, Ayabe T, Aizawa T.
  Antibiotics (Basel), 12, 1047 (2023)


• Structure and Heterogeneity of Retinal Chromophore in Chloride Pump Rhodopsins Revealed by Raman Optical Activity
  Ohya M, Kikukawa T, Matsuo J, Tsukamoto T, Nagaura R, Fujisawa T, Unno M.
  J Phys Chem B., 127, 4775-4782 (2023)


• Elucidation of a Thermodynamical Feature Attributed to Substrate Binding to the Prokaryotic H+/Oligopeptide Cotransporter YdgR with Calorimetric Analysis: The Substrate Binding Driven by the Change in Entropy Implies the Release of Bound Water Molecules from the Binding Pocket
  Omori A, Sasaki S, Kikukawa T, Shimono K, Miyauchi S.
  Biochemistry, 62, 1608-1618 (2023)


• Phenylazothiazoles as Visible-Light Photoswitches
  Lin R, Hashim PK, Sahu S, Amrutha AS, Cheruthu NM, Thazhathethil S, Takahashi K, Nakamura T, Kikukawa T, Tamaoki N.
  J. Am. Chem. Soc., 145, 9072-9080 (2023)


• Efficient recombinant production of mouse-derived cryptdin family peptides by a novel facilitation strategy for inclusion body formation
  Song, Y., Wang, Y., Yan, S., Nakamura, K., Kikukawa, T., Ayabe, T., Aizawa, T.
  Microb. Cell Fact., 22, 9 (2023)

2022

• Mutations conferring SO42− pumping ability on the cyanobacterial anion pump rhodopsin and the resultant unique features of the mutant
  Y. Doi, J. Watanabe, R. Nii, T. Tsukamoto, M. Demura, Y. Sudo, T. Kikukawa
  Sci Rep., 12, 16422 (2022)


• Reisomerization of retinal represents a molecular switch mediating Na⁺ uptake and release by a bacterial sodium-pumping rhodopsin
  T. Fujisawa, K. Kinoue, R. Seike, T. Kikukawa, M. Unno
  J. Biol. Chem., 296, 102366 (2022)


• Three-Dimensional Structure of the Antimicrobial Peptide Cecropin P1 in Dodecylphosphocholine Micelles and the Role of the C-Terminal Residues
  Gu. H., Kato, T., Kumeta, H., Kumaki, Y., Tsukamoto, T., Kikukawa, T., Demura, M., Ishida, H., Vogel, H.J., Aizawa, T.
  ACS Omega, 7, 31924-31934 (2022)


• Potent bactericidal activity of reduced cryptdin-4 derived from its hydrophobicity and mediated by bacterial membrane disruption
  Sato, Y., Wang, Y., Song, Y., Geng, W., Yan, S., Nakamura, K., Kikukawa, T., Demura, M., Ayabe, T., Aizawa, T.
  Amino Acids, 54, 289-297 (2022)

2021

• Pore Size Distributions Related with Spontaneous Purple Membrane Stacking in Porous Hydrogels
  M. Karasawa, Y. Yokoyama, K. Takiguchi, H. Takahashi, T. Kikukawa, M. Sonoyama, K. Takenaka
  J. Phys. Soc. Jpn., 90, 103801 (2021)


• Replaceability of Schiff base proton donors in light-driven proton pump rhodopsins
  S. Sasaki, J. Tamogami, K. Nishiya, M. Demura, T. Kikukawa
  J. Biol. Chem., 97, 101013 (2021)


• Functional expression of the eukaryotic proton pump rhodopsin OmR2 in Escherichia coli and its photochemical characterization
  M. Kikuchi, K. Kojima, S. Nakao, S. Yoshizawa, S. Kawanishi, A. Shibukawa, T. Kikukawa, Y. Sudo
  Sci Rep. , 11, 14765 (2021)


• Comparison of Functionality and Structural Stability of Bacteriorhodopsin Reconstituted in Partially Fluorinated Dimyristoylphosphatidylcholine Liposomes with Different Perfluoroalkyl Chain Lengths
  M. Hashimoto, Y. Murai, K. Morita, T. Kikukawa, T. Takagi, H. Takahashi, Y. Yokoyama, H. Amii, M. Sonoyama
  Biochim. Biophys. Acta, Biomembr., 1863, 183686 (2021)


• Spectroscopic approach for exploring structure and function of photoreceptor proteins
  Unno, M., Hirose, Y., Mishima, M., Kikukawa, T., Fujisawa, T., Iwata, T., Tamogami, J.
  Biophys. Physicobiol., 18, 127-130 (2021)


• Protonation State of a Histidine Residue in Human Oligopeptide Transporter 1 (hPEPT1) Regulates hPEPT1-Mediated Efflux Activity
  A. Omori, Y. Fujisawa, S. Sasaki, K. Shimono, T. Kikukawa, S. Miyauchi
  Biol. Pharm. Bull., 44, 678-685 (2021)


• Real-Time Identification of Two Substrate-Binding Intermediates for the Light-Driven Sodium Pump Rhodopsin
  T. Kato, T. Tsukamoto, M. Demura, T. Kikukawa
  J. Biol. Chem., 296, 100792 (2021)


• Preference of Proteomonas sulcata anion channelrhodopsin for NO₃⁻ revealed using a pH electrode method
  C. Kikuchi, H. Kurane, T. Watanabe, M. Demura, T. Kikukawa, T. Tsukamoto
  Sci Rep. , 11, 7908 (2021)


• Effects of salt and gel network structures on purple membrane stacking in hydrogels immobilized with poly(vinyl alcohol)
  Y. Yokoyama, S. Yano, R. Kurita, M. Karasawa, H. Tanaka, H. Takahashi, T. Kikukawa, M. Sonoyama, K. Takenaka
  J. Appl. Phys., 129, 014701 (2021)


• Low-temperature Raman spectroscopy of sodium-pump rhodopsin from Indibacter alkaliphilus: Insight of Na+ binding for active Na+ transport
  Y. Nakamizo, T. Fujisawa, T. Kikukawa, A. Okamura, H. Baba, M. Unno
  Phys. Chem. Chem. Phys., 23, 2072-2079 (2021)

2020

• Lokiarchaeota archaeon schizorhodopsin-2 (LaSzR2) is an inward proton pump displaying a characteristic feature of acid-induced spectral blue-shift
  K. Kojima, S. Yoshizawa, M. Hasegawa, M. Nakama, M. Kurihara, T. Kikukawa, Y. Sudo
  Sci Rep. , 10, 20857 (2020)


• “Watching” a Molecular Twist in a Protein by Raman Optical Activity
  J. Matsu, T. Kikukawa, T. Fujisawa, W. D. Hoff, M. Unno
  J. Phys. Chem. Lett., 11, 8579–8584


• Direct Detection of the Substrate Uptake and Release Reactions of the Light-Driven Sodium-Pump Rhodopsin.
  K. Murabe, T. Tsukamoto, T. Aizawa, M. Demura, T. Kikukawa
  J Am Chem Soc., 142, 16023-16030 (2020)


• Spectroscopic Characterization of Halorhodopsin Reconstituted into Nanodisks Using Native Lipids.
  A. Yamamoto, T. Tsukamoto, K. Suzuki, E. Hashimoto, Y. Kobashigawa, K. Shibasaki, T. Uchida, F. Inagaki, M. Demura, K. Ishimori
  Biophys J., 118, 2853-2865 (2020)


• Methodology for Further Thermostabilization of an Intrinsically Thermostable Membrane Protein Using Amino Acid Mutations with Its Original Function Being Retained
  S. Yasuda, T. Akiyama, S. Nemoto, T. Hayashi, T. Ueta, K. Kojima, T. Tsukamoto, S. Nagatoishi, K. Tsumoto, Y. Sudo, M. Kinoshita, T. Murata
  J. Chem. Inf. and Model., 60, 1709-1716 (2020)

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解説・総説など

• 1) 菊川峰志, 尾瀬農之, 金城政孝, 「蛍光偏光測定」、津本浩平・前仲勝実（編）、実験医学別冊「創薬研究のための相互作用解析パーフェクト : 低中分子・抗体創薬におけるスクリーニング戦略と実例、in silico解析、一歩進んだ分析技術まで」, pp. 74-85, ISBN: 978-4-7581-2256-6, 洋土社. (2021)
• Tamogami, J., Kikukawa, T., Functional Mechanism of Proton Pump-Type Rhodopsins Found in Various Microorganisms as a Potential Effective Tool, In Epigenetics to Optogenetics - A New Paradigm in the Study of Biology (Anwar, M., Farooq, Z., Rather, R.A., Tauseef, M., Heinbockel, T., Eds.), IntechOpen (2021)
• Kikukawa, T., Unique Cl^- pump rhodopsin with close similarity to H⁺ pump rhodopsin, Biophys. Physicobiol., Vol.18, 317-326 (2021)
• 菊川峰志, Cl^–ポンプロドプシンの分子機構とH⁺ポンプへの機能変換, 生物物理 61: 12-15 (2021)
• Kikukawa, T., Functional Mechanism of Cl⁻-Pump Rhodopsin and Its Conversion into H⁺ Pump, In Optogenetics 2nd Ed.: Light-Sensing Proteins and Their Applications in Neuroscience and Beyond (Yawo., H., Kandori, H., Koizumi, A., Kageyama, R., Eds.), pp 55-71, ISBN: 978-981-15-8763-4, Springer (2021)
• 菊川峰志, プロテオロドプシン, 「光と生命の事典」, pp. 58-59, ISBN: 978-4-254-17161-7, 朝倉書店 (2016)
• Takashi Kikukawa, Naoki Kamo and Makoto Demura, Photochemistry of Halorhodopsin in Optogenetics (Eds. Hideki Kandori, Hiromu Yawo, Amane Koizumi) Springer 2015, pp47-62.

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