ISHIKAWA, Haruto - Osaka University - Department of Chemistry

个人简介

Education Ph. D., Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, 2003. M. Eng., Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, 1999. B. Eng., Department of Industrial Chemistry, Fuculty of Engineering, Kyoto University, 1997. Professional Experiences March 2010-present; Associate Professor: Graduate School of Science, Osaka University April 2009-March 2010; Research Assistance Professor: Okazaki Institute for Integrative Bioscience April 2008-March 2009; Postdoctoral Research Fellow: Graduate School of Science, Osaka University October 2005-March 2008; Postdoctoral Research Fellow: Department of Chemistry, Stanford University April 2003-September 2005; Postdoctoral Research Fellow: Department of Molecular Cell Biology, Osaka City University April 2006-March 2009; Postdoctoral Research Fellow: Human Frontier Science Program Long-Term Fellow April 2003-March 2006; Postdoctoral Research Fellow: Japan Society for the Promotion of Science (PD) April 1999-March 2002; Postdoctoral Research Fellow: Japan Society for the Promotion of Science (DC1) Honors and Awards 2006年 Human Frontier Science Program Long-Term Fellow 2009年 Human Frontier Science Program Career Development Award

研究领域

Protein dynamics are intimately connected to the structure/function relationship of biological systems. In numerous biological processes, the ensuing protein structural changes accompanying a reaction at a specific site must spatially extend to the mesoscopic dimensions of the protein to achieve a biological function. The molecular mechanism of cooperativity in oxygen binding of hemoglobin is one of the classical problems in this aspect. The large-amplitude motions at the quaternary level, which form a communication link at the subunit interface, are driven by changes in the tertiary structure upon ligation. Protein dynamics spans over a wide range of time scales. To answer questions on protein dynamics, we need the concatenation of experimental results recorded over many orders of magnitude of time. In this regard it is important that a single experimental technique can examine protein structures evolving from the earliest moments, such as the picosecond regime, toward time scales that are highly relevant to biological functions, such as the microsecond or millisecond regimes. One might ask whether ultrafast spectroscopy can provide anything to understand protein systems. There are some good reasons for us to believe that the answer is positive. One method for studying the dynamic motions of proteins is to pursue the ensuing relaxation after shifting a protein from equilibrium. If we use short pulses to initiate a very rapid photoreaction at an active site, immediately after the start of a reaction, the result is a metastable structure whose active site is different but the tertiary and quaternary structures of the protein are similar to the original state. The surrounding “protein solvent” is now the structural variable. A short probe pulse following the initiating pulse provides direct information on the relaxation of this metastable form into the equilibrium protein structure. In this way, the quickest responses of proteins can be monitored by ultrafast spectroscopy. Another feature to be noted about ultrafast spectroscopy is the possibility of studying energy dissipation in proteins, which is very important to understanding reactions in proteins. In general, energy dissipation occurs in the sub-picosecond to picosecond regime in the condensed phases. Ultrafast spectroscopy is required in order to study how the deposited energy dissipates in proteins. In addition to such relaxation processes, there are conformational fluctuations around the equilibrium points. The tertiary structure is undergoing fluctuations on a time scale of hindered molecular rotations. These motions can also be studied by various ultrafast spectroscopic techniques. Research Subjects Structural chemistry on allosteric proteins Functionally-important structural fluctuation of protein Photoscience of protein Development of techniques for time-resolved spectroscopy

近期论文

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""Differences between Protein Dynamics of Hemoglobin upon Dissociation of Oxygen and Carbon Monoxide"", Yuka Murakawa, Masako Nagai and Yasuhisa Mizutani, J. Am. Chem. Soc., 134, 1434-1437 (2012). ""Ultrafast Protein Dynamics of Hemoglobin as Studied by Picosecond Time-resolved Resonance Raman Spectroscopy"", Yasuhisa Mizutani and Masako Nagai, Chem. Phys., 396, 45-52 (2012). ""Protein Dynamics of Isolated Chains of Recombinant Human Hemoglobin Elucidated by Time-resolved Resonance Raman Spectroscopy"", Kenta Yamada, Haruto Ishikawa, and Yasuhisa Mizutani, J. Phys. Chem. B, 116, 1992–1998 (2012). ""Protein dynamics of heme-heme oxygenase-1 complex following carbon monoxide dissociation"", Masato Yamaoka, Masakazu Sugishima, Masato Noguchi, Keiichi Fukuyama and Yasuhisa Mizutani, J. Raman Spectrosc., 42, 910–916 (2011). ""Direct observation of the structural change of Tyr174 in the primary reaction of sensory rhodopsin II"", Misao Mizuno*, Yuki Sudo*, Michio Homma and Yasuhisa Mizutani, Biochemistry, 50, 3170–3180 (2011). ""Changes in the Hydrogen-Bond Network around the Chromophore of Photoactive Yellow Protein in the Ground and Excited States"", Misao Mizuno, Hironari Kamikubo, Mikio Kataoka and Yasuhisa Mizutani, J. Phys. Chem. B, 115, 9306–9310 (2011). ""Direct observation of vibrational energy flow in cytochrome c"", Naoki Fujii, Misao Mizuno, and Yasuhisa Mizutani, J. Phys. Chem. B, 115, 13057–13064 (2011). ""Protein Conformational Changes in the Oxidative-Stress Sensor, SoxR, upon Redox Change of the [2Fe-2S] Cluster Probed with Ultraviolet Resonance Raman Spectroscopy"", Kazuo Kobayashi, Misao Mizuno, and Yasuhisa Mizutani, Biochemistry, 50, 9468–9474 (2011). ""Picosecond Time-Resolved Ultraviolet Resonance Raman Spectroscopy of Bacteriorhodopsin: Primary Protein Response to the Photoisomerization of Retinal"", Misao Mizuno, Mikihiro Shibata, Junya Yamada, Hideki Kandori, and Yasuhisa Mizutani, J. Phys. Chem. B, 113, 12121–12128 (2009). ""Photoinduced Dynamics of TiO2 Doped with Cr and Sb"", Toshitatsu Ikeda, Tomonori Nomoto, Kazuo Eda, Yasuhisa Mizutani, Hideki Kato, Akihiko Kudo, and Hiroshi Onishi, J. Phys. Chem. C, 112, 1167 -1173 (2008). ""Ruthenium-Catalyzed Selective and Efficient Oxygenation of Hydrocarbons with Water as an Oxygen Source"", Takahiko Kojima, Yuichirou Hirai, Yasuhisa Mizutani, Yoshihito Shiota, Kazunari Yoshizawa, Shunichi Fukuzumi, Angew. Chem. Int. Ed., 47, 5772-5776 (2008). ""Photoinduced Electron Transfer in Glucose Oxidase: a Picosecond Time-resolved Ultraviolet Resonance Raman Study"", Akiko Fujiwara and Yasuhisa Mizutani, J. Raman Spectrosc., 39, 1600-1605 (2008). ""Resonance Raman Observation of the Structural Dynamics of FixL on Ligand Recognition and Signaling"", Yusuke Hiruma, Akihiro Kikuchi, Atsunari Tanaka, Yoshitsugu Shiro, and Yasuhisa Mizutani, Biochemistry, 46, 6086-6096 (2007). ""The Formation of Hydrogen Bond in the Proximal Heme Pocket of HemAT-Bs upon Ligand Binding"", Hideaki Yoshimura, Shiro Yoshioka, Yasuhisa Mizutani, and Shigetoshi Aono, Biochem. Biophys. Res. Commun., 357, 1053-1057 (2007). ""Picosecond Protein Response to the Chromophore Isomerization of Photoactive Yellow Protein: Selective Observation of Tyrosine and Tryptophan Residues by Time-Resolved Ultraviolet Resonance Raman Spectroscopy"", Misao Mizuno, Norio Hamada, Fumio Tokunaga, and Yasuhisa Mizutani, J. Phys. Chem. B, 111, 6293-6296 (2007). ""Primary protein response after ligand photodissociation in carbonmonoxy myoglobin"", Akira Sato, Ying Gao, Teizo Kitagawa, and Yasuhisa Mizutani, Proc. Natl. Acad. Sci. USA, 104, 9627-9632 (2007). ""Time-resolved Raman Evidence for Energy ""Funneling"" through Propionate Side Chains in Heme ""Cooling"" upon Photolysis of Carbonmonoxy Myoglobin"", Ying Gao, Mai Koyama, Samir F. El-Mashtoly, Takashi Hayashi, Katsuyoshi Harada, Yasuhisa Mizutani and Teizo Kitagawa, Chem. Phys. Lett., 429, 239-243 (2006). ""Role of heme propionates of myoglobin in vibrational energy relaxation"", Mai Koyama, Saburo Neya, and Yasuhisa Mizutani, Chem. Phys. Lett., 430, 404-408 (2006). ""Evidence for Displacements of C-Helix by CO Ligation and DNA Binding to CooA Revealed by UV Resonance Raman Spectroscopy"", Minoru Kubo, Sayaka Inagaki, Takeshi Uchida, Yasuhisa Mizutani, Shigetoshi Aono, and Teizo Kitagawa, J. Biol. Chem., 281, 11271-11278 (2006). ""Picosecond Structural Dynamics of Myoglobin following Photodissociation of Carbon Monoxide As Revealed by Ultraviolet Time-Resolved Resonance Raman Spectroscopy"", Akira Sato and Yasuhisa Mizutani, Biochemistry 44, 14709-14714 (2005).