Unique Photochemistry Observed in a New Microbial Rhodopsin

Chihiro Kataoka; Keiichi Inoue; Kota Katayama; Oded Beja; Hideki Kandori

doi:https://doi.org/10.1021/acs.jpclett.9b01957

Unique Photochemistry Observed in a New Microbial Rhodopsin

Chihiro Kataoka, Keiichi Inoue, Kota Katayama, Oded Beja, Hideki Kandori

Technion - Israel Institute of Technology

Research output: Contribution to journal › Article › peer-review

Abstract

Light energy is first captured in animal and microbial rhodopsins by ultrafast photoisomerization, whose relaxation accompanies protein structural changes for each function. Here, we report a microbial rhodopsin, marine bacterial TAT rhodopsin, that displays no formation of photointermediates at >10^-5 s. Low-temperature ultraviolet-visible and Fourier transform infrared spectroscopy revealed that TAT rhodopsin features all-trans to 13-cis photoisomerization like other microbial rhodopsins, but a planar 13-cis chromophore in the primary K intermediate seems to favor thermal back isomerization to the original state without photocycle completion. The molecular mechanism of the early photoreaction in TAT rhodopsin will be discussed.

Original language	English
Pages (from-to)	5117-5121
Number of pages	5
Journal	Journal of Physical Chemistry Letters
Volume	10
Issue number	17
DOIs	https://doi.org/10.1021/acs.jpclett.9b01957
State	Published - 5 Sep 2019

All Science Journal Classification (ASJC) codes

General Materials Science
Physical and Theoretical Chemistry

Access to Document

https://doi.org/10.1021/acs.jpclett.9b01957

Cite this

@article{67b5b48b3540444c865b090ab7457574,

title = "Unique Photochemistry Observed in a New Microbial Rhodopsin",

abstract = "Light energy is first captured in animal and microbial rhodopsins by ultrafast photoisomerization, whose relaxation accompanies protein structural changes for each function. Here, we report a microbial rhodopsin, marine bacterial TAT rhodopsin, that displays no formation of photointermediates at >10-5 s. Low-temperature ultraviolet-visible and Fourier transform infrared spectroscopy revealed that TAT rhodopsin features all-trans to 13-cis photoisomerization like other microbial rhodopsins, but a planar 13-cis chromophore in the primary K intermediate seems to favor thermal back isomerization to the original state without photocycle completion. The molecular mechanism of the early photoreaction in TAT rhodopsin will be discussed.",

author = "Chihiro Kataoka and Keiichi Inoue and Kota Katayama and Oded Beja and Hideki Kandori",

note = "Publisher Copyright: Copyright {\textcopyright} 2019 American Chemical Society.",

year = "2019",

month = sep,

day = "5",

doi = "https://doi.org/10.1021/acs.jpclett.9b01957",

language = "الإنجليزيّة",

volume = "10",

pages = "5117--5121",

journal = "Journal of Physical Chemistry Letters",

issn = "1948-7185",

publisher = "American Chemical Society",

number = "17",

}

TY - JOUR

T1 - Unique Photochemistry Observed in a New Microbial Rhodopsin

AU - Kataoka, Chihiro

AU - Inoue, Keiichi

AU - Katayama, Kota

AU - Beja, Oded

AU - Kandori, Hideki

PY - 2019/9/5

Y1 - 2019/9/5

N2 - Light energy is first captured in animal and microbial rhodopsins by ultrafast photoisomerization, whose relaxation accompanies protein structural changes for each function. Here, we report a microbial rhodopsin, marine bacterial TAT rhodopsin, that displays no formation of photointermediates at >10-5 s. Low-temperature ultraviolet-visible and Fourier transform infrared spectroscopy revealed that TAT rhodopsin features all-trans to 13-cis photoisomerization like other microbial rhodopsins, but a planar 13-cis chromophore in the primary K intermediate seems to favor thermal back isomerization to the original state without photocycle completion. The molecular mechanism of the early photoreaction in TAT rhodopsin will be discussed.

AB - Light energy is first captured in animal and microbial rhodopsins by ultrafast photoisomerization, whose relaxation accompanies protein structural changes for each function. Here, we report a microbial rhodopsin, marine bacterial TAT rhodopsin, that displays no formation of photointermediates at >10-5 s. Low-temperature ultraviolet-visible and Fourier transform infrared spectroscopy revealed that TAT rhodopsin features all-trans to 13-cis photoisomerization like other microbial rhodopsins, but a planar 13-cis chromophore in the primary K intermediate seems to favor thermal back isomerization to the original state without photocycle completion. The molecular mechanism of the early photoreaction in TAT rhodopsin will be discussed.

UR - http://www.scopus.com/inward/record.url?scp=85072065932&partnerID=8YFLogxK

U2 - https://doi.org/10.1021/acs.jpclett.9b01957

DO - https://doi.org/10.1021/acs.jpclett.9b01957

M3 - مقالة

SN - 1948-7185

VL - 10

SP - 5117

EP - 5121

JO - Journal of Physical Chemistry Letters

JF - Journal of Physical Chemistry Letters

IS - 17

ER -

Unique Photochemistry Observed in a New Microbial Rhodopsin

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this