Absorption spectra and photochemical reactions in a unique photoactive protein, middle rhodopsin MR

Keiichi Inoue, Louisa Reissig, Makoto Sakai, Shiori Kobayashi, Michio Homma, Masaaki Fujii, Hideki Kandori, Yuki Sudo

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Photoactive proteins with cognate chromophores are widespread in organisms, and function as lightenergy converters or receptors for light-signal transduction. Rhodopsins, which have retinal (vitamin A aldehyde) as their chromophore within their seven transmembrane α-helices, are classified into two groups, microbial (type-1) and animal (type-2) rhodopsins. In general, light absorption by type-1 or type-2 rhodopsins triggers a trans-cis or cis-trans isomerization of the retinal, respectively, initiating their photochemical reactions. Recently, we found a new microbial rhodopsin (middle rhodopsin, MR), binding three types of retinal isomers in its original state: all-trans, 13-cis, and 11-cis. Here, we identified the absolute absorption spectra of MR by a combination of high performance liquid chromatography (HPLC) and UV-vis spectroscopy under varying light conditions. The absorption maxima of MR with all-trans, 13-cis, or 11-cis retinal are located at 485, 479, and 495 nm, respectively. Their photocycles were analyzed by time-resolved laser spectroscopy using various laser wavelengths. In conclusion, we propose that the photocycles of MR are MR(trans) → MRK:lifetime = 93 μs → MRM:lifetime = 12 ms → MR, MR(13-cis) → MR O-like:lifetime = 5.1 ms → MR, and MR(11-cis) → MR K-like:lifetime = 8.2 μs → MR, respectively. Thus, we demonstrate that a single photoactive protein drives three independent photochemical reactions.

Original languageEnglish
Pages (from-to)5888-5899
Number of pages12
JournalJournal of Physical Chemistry B
Volume116
Issue number20
DOIs
Publication statusPublished - Mar 24 2012
Externally publishedYes

Fingerprint

Rhodopsin
Photochemical reactions
Chromophores
photochemical reactions
Absorption spectra
proteins
Proteins
absorption spectra
life (durability)
Signal transduction
Laser spectroscopy
Vitamins
High performance liquid chromatography
Isomerization
Ultraviolet spectroscopy
Aldehydes
Isomers
Light absorption
chromophores
Animals

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Materials Chemistry
  • Surfaces, Coatings and Films

Cite this

Absorption spectra and photochemical reactions in a unique photoactive protein, middle rhodopsin MR. / Inoue, Keiichi; Reissig, Louisa; Sakai, Makoto; Kobayashi, Shiori; Homma, Michio; Fujii, Masaaki; Kandori, Hideki; Sudo, Yuki.

In: Journal of Physical Chemistry B, Vol. 116, No. 20, 24.03.2012, p. 5888-5899.

Research output: Contribution to journalArticle

Inoue, K, Reissig, L, Sakai, M, Kobayashi, S, Homma, M, Fujii, M, Kandori, H & Sudo, Y 2012, 'Absorption spectra and photochemical reactions in a unique photoactive protein, middle rhodopsin MR', Journal of Physical Chemistry B, vol. 116, no. 20, pp. 5888-5899. https://doi.org/10.1021/jp302357m
Inoue, Keiichi ; Reissig, Louisa ; Sakai, Makoto ; Kobayashi, Shiori ; Homma, Michio ; Fujii, Masaaki ; Kandori, Hideki ; Sudo, Yuki. / Absorption spectra and photochemical reactions in a unique photoactive protein, middle rhodopsin MR. In: Journal of Physical Chemistry B. 2012 ; Vol. 116, No. 20. pp. 5888-5899.
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