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B: Biophysics; Physical Chemistry of Biological Systems and Biomolecules
Ultrafast Dynamics of Heliorhodopsins Shinya Tahara, Manish Singh, Hikaru Kuramochi, Wataru Shihoya, Keiichi Inoue, Osamu Nureki, Oded Béjà, Yasuhisa Mizutani, Hideki Kandori, and Tahei Tahara J. Phys. Chem. B, Just Accepted Manuscript • Publication Date (Web): 11 Feb 2019 Downloaded from http://pubs.acs.org on February 11, 2019
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The Journal of Physical Chemistry
Ultrafast Dynamics of Heliorhodopsins Shinya Taharaa, Manish Singhb, Hikaru Kuramochic,d,e, Wataru Shihoyaf, Keiichi Inouee,g, Osamu Nurekif, Oded Béjàh, Yasuhisa Mizutania, Hideki Kandorib,i, Tahei Tahara*c,d
aDepartment
of Chemistry, Graduate School of Science, Osaka University, 1-1
Machikaneyama, Toyonaka, Osaka 560-0043, Japan
bDepartment
of Life Science and Applied Chemistry, Nagoya Institute of Technology,
Showa-ku, Nagoya 466-8555, Japan
cMolecular
dUltrafast
Spectroscopy Laboratory, RIKEN, 2-1 Hirosawa, Wako 351-0198, Japan
Spectroscopy Research Team, RIKEN Center for Advanced Photonics (RAP),
2-1 Hirosawa, Wako 351-0198, Japan
ePRESTO,
Japan Science and Technology Agency, 4-1-8 Honcho Kawaguchi, Saitama
332-0012, Japan
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fDepartment
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of Biological Sciences, Graduate School of Science, The University of
Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
gInstitute
for Solid State Physics, The University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa,
Chiba 277-8581, Japan
hFaculty
of Biology, Technion Israel Institute of Technology, Haifa 32000, Israel
iOptoBioTechnology
Research Center, Nagoya Institute of Technology, Showa-ku,
Nagoya 466-8555, Japan
ABSTRACT
Heliorhodopsins (HeR) constitute a new rhodopsin family and show only 650 nm region, and these transient signals decay concomitantly with appearance of photoproduct absorption on a sub-picosecond timescale.
The
observed
spectral
change
indicates
that
ultrafast
retinal
photoisomerization proceeds in the femtosecond time region. The transient spectra and dynamics of HeRs are surprisingly similar to those of type-1 rhodopsins, despite remarkable differences in amino acid arrangement in the hydrophobic region of the retinal binding site.
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INTRODUCTION Rhodopsins, which have been found in a wide variety of organisms,1 are classified into type-1 and type-2.
Type-1 rhodopsins are microbial rhodopsins whereas type-2
rhodopsins are rhodopsins relevant to animal vision. Type-1 and type-2 rhodopsins have all-trans and 11-cis retinal chromophore, respectively, and they commonly have seven trans-membrane helices despite no sequence similarity. Very recently, a new type of rhodopsins, heliorhodopsin (HeR), was discovered by a functional metagenomic analysis. Although HeRs have an all-trans retinal chromophore as in the case of type-1 rhodopsin, they show only
