Yuki Sudo
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Research Subjects
Research Interests
Yuki Sudo has a total of 18 co-authors. Here are the top co-authors by number of shared publications:
- Kazumi Shimono
RIKEN Systems and Structural Biology Center, Yokohama 230-0045, Japan
3 shared publications - Masayuki Iwamoto
Laboratory of Biomolecular Systems, Center for Advanced Science and Technology, Hokkaido University, Sapporo 001-0021, Japan
3 shared publications - Naoki Kamo
Grad. Sch. Life Sci., Hokkaido Univ
3 shared publications Naoki Kamo
Matsuyama University
2 shared publicationsYukako Ikeura
Laboratory of Biophysical Chemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan
2 shared publications- Akimori Wada
Laboratory of Organic Chemistry for Life Science, Kobe Pharmaceutical University, Kobe 658-8558, Japan
1 shared publication
Latest Publications
- 1 January 2012
- Published by Biophysical Society of Japan in Seibutsu Butsuri
- Vol. 52 (supplement)
1F1558 Light activated states of photoreceptor membrane proteins as revealed by in-situ photo-irradiated solid-state NMR(Photobiology: Vision & Photoreception I,Oral Presentation,The 50th Annual Meeting of the Biophysical Society of Japan)
- 1 January 2012
- Published by Biophysical Society of Japan in Seibutsu Butsuri
- Vol. 52 (supplement)
1F1558 Light activated states of photoreceptor membrane proteins as revealed by in-situ photo-irradiated solid-state NMR(Photobiology: Vision & Photoreception I,Oral Presentation,The 50th Annual Meeting of the Biophysical Society of Japan)
- 1 April 2006
- Published by Elsevier in Journal of Molecular Biology
- Vol. 357 (4) , 1274-1282
Importance of Specific Hydrogen Bonds of Archaeal Rhodopsins for the Binding to the Transducer Protein
- 1 April 2006
- Published by Elsevier in Journal of Molecular Biology
- Vol. 357 (4) , 1274-1282
Importance of Specific Hydrogen Bonds of Archaeal Rhodopsins for the Binding to the Transducer Protein
- 1 January 2003
- Published by Wiley in Photochemistry and Photobiology
- Vol. 77 (1) , 96
Arg-72 of pharaonis Phoborhodopsin (Sensory Rhodopsin II) is Important for the Maintenance of the Protein Structure in the Solubilized State¶
- 1 January 2003
- Published by Wiley in Photochemistry and Photobiology
- Vol. 77 (1) , 96
Arg-72 of pharaonis Phoborhodopsin (Sensory Rhodopsin II) is Important for the Maintenance of the Protein Structure in the Solubilized State¶
- 1 January 2002
- Published by Wiley in Photochemistry and Photobiology
- Vol. 76 (4) , 462-6
Illumination Accelerates the Decay of the O-intermediate of pharaonis Phoborhodopsin (Sensory Rhodopsin II)¶
Pharaonis phoborhodopsin (ppR, also called pharaonis sensory rhodopsin II [psRII]) is a member of the archaeal rhodopsin family and acts as a repellent phototaxis receptor of Natronobacterium pharaonis. Upon illumination, ppR is excited and undergoes a linear cyclic photoreaction, namely, a photocycle that constitutes photointermediates such as M- and O-intermediates (ppRM and ppRO, respectively). Under a constant background illumination (>600 nm) that irradiates ppRO, the decay rate of the flash-induced ppRO increased with an increase in the background light intensity, indicating the photoreactivity of ppRO. Azide did not influence the light-accelerated ppRO decay, but the time required for the cycle to be completed became shortened in an azide concentration-dependent manner because of acceleration of ppRM decay. Hence, the turnover rate of photocycling increased appreciably in the presence of both the background illumination and the azide. The observation reported previously (Schmies, G. et al. 2000, Biophys. J. 78:967-976) is discussed in connection with the present observations.
- 1 January 2002
- Published by Wiley in Photochemistry and Photobiology
- Vol. 76 (4) , 462-6
Illumination Accelerates the Decay of the O-intermediate of pharaonis Phoborhodopsin (Sensory Rhodopsin II)¶
Pharaonis phoborhodopsin (ppR, also called pharaonis sensory rhodopsin II [psRII]) is a member of the archaeal rhodopsin family and acts as a repellent phototaxis receptor of Natronobacterium pharaonis. Upon illumination, ppR is excited and undergoes a linear cyclic photoreaction, namely, a photocycle that constitutes photointermediates such as M- and O-intermediates (ppRM and ppRO, respectively). Under a constant background illumination (>600 nm) that irradiates ppRO, the decay rate of the flash-induced ppRO increased with an increase in the background light intensity, indicating the photoreactivity of ppRO. Azide did not influence the light-accelerated ppRO decay, but the time required for the cycle to be completed became shortened in an azide concentration-dependent manner because of acceleration of ppRM decay. Hence, the turnover rate of photocycling increased appreciably in the presence of both the background illumination and the azide. The observation reported previously (Schmies, G. et al. 2000, Biophys. J. 78:967-976) is discussed in connection with the present observations.