Laboratory of Biological Information Analysis Science
- Research Theme
- Elucidation of the light-energy conversion mechanisms of photoactive proteins / Development of photoactive systems by featuring functionally modified photoactive proteins
- Research Keywords
Photoactive proteins, photobiology, rhodopsin, optogenetics, laboratory evolution, membrane protein, ion pump, membrane transport, transporter, flash photolysis
Staff
Overview of Research and Education
Organisms express photoactive proteins to utilize sunlight for cellular metabolic processes. Rhodopsins are the most ubiquitous photoactive proteins and have diverse functions, such as photosensors, ion pumps, and ion channels. We are analyzing their essential mechanisms for light-energy utilization and functional differentiation. Our goal is to develop the novel photoactive proteins applicable to environmental and medical problems.
Laboratory of Biological Information Analysis Science (pdf)
Charge
- Charge (US):
School of Science, Biological Science course (Macromolecular Functions), Core Laboratories - Charge (GS):
Graduate School of Life Science, Division of Soft Matter, Biomolecular Soft Matter
Contact
- Address
- 〒060-0810
N10, W8, Kita-ku, Sapporo, Hokkaido - Phone
- 011-706-2771
- Fax
- 011-706-2771
- demura*sci.hokudai.ac.jp (Please replace ＊ with @ when sending e-mail.)
Representative Publications
Sasaki, S., Tamogami, J., Nishiya, K., Demura, M., Kikukawa, T., Replaceability of Schiff base proton donors in light-driven proton pump rhodopsins, J. Biol. Chem. 297, 101013 (2021)
Kato, T., Tsukamoto, T., Demura, M., Kikukawa, T., Real-time identification of two substrate-binding intermediates for the light-driven sodium pump rhodopsin, J. Biol. Chem. 296, 100792 (2021)
Kikuchi, C., Kurane, H., Watanabe, T., Demura, M., Kikukawa, T., Tsukamoto, T., Preference of Proteomonas sulcata anion channelrhodopsin for NO3− revealed using a pH electrode method, Sci. Rep. 11, 7908 (2021)
Murabe, K., Tsukamoto, T., Aizawa, T., Demura, M., Kikukawa, T., Direct Detection of the Substrate Uptake and Release Reactions of the Light-Driven Sodium-Pump Rhodopsin, J. Am. Chem. Soc. 142: 16023-16030 (2020)
Iizuka, A., Kajimoto, K., Fujisawa, T., Tsukamoto, T., Aizawa, T., Kamo, N., Jung, KH, Unno, M., Demura, M., Kikukawa, T., Functional importance of the oligomer formation of the cyanobacterial H+ pump Gloeobacter rhodopsin, Sci. Rep. 9: 10711 (2019)
Tsukamoto, T., Kikuchi, C., Suzuki, H., Aizawa, T., Kikukawa, T., Demura, M., Implications for the impairment of the rapid channel closing of Proteomonas sulcata anion channelrhodopsin 1 at high Cl- concentrations, Sci. Rep., 8: 13445 (2018)
Hasemi, T., Kikukawa, T., Kamo, N., Demura, M., Characterization of a Cyanobacterial Chloride-Pumping Rhodopsin and its Conversion into a Proton Pump, J. Biol. Chem. 291: 355-362 (2016)