Role of Thr82 for the unique photochemistry of TAT rhodopsin.

photocycle photoisomerization protonation retinal rhodopsin

Journal

Biophysics and physicobiology
ISSN: 2189-4779
Titre abrégé: Biophys Physicobiol
Pays: Japan
ID NLM: 101675089

Informations de publication

Date de publication:
2021
Historique:
received: 12 03 2021
accepted: 14 04 2021
entrez: 24 5 2021
pubmed: 25 5 2021
medline: 25 5 2021
Statut: epublish

Résumé

Marine bacterial TAT rhodopsin possesses the pKa of the retinal Schiff base, the chromophore, at neutral pH, and photoexcitation of the visible protonated state forms the isomerized 13-

Identifiants

pubmed: 34026400
doi: 10.2142/biophysico.bppb-v18.012
pii: JST.JSTAGE/biophysico/bppb-v18.012
pmc: PMC8116198
doi:

Types de publication

Journal Article

Langues

eng

Pagination

108-115

Informations de copyright

2021 THE BIOPHYSICAL SOCIETY OF JAPAN.

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Auteurs

Teppei Sugimoto (T)

Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Nagoya, Aichi 466-8555, Japan.

Kota Katayama (K)

Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Nagoya, Aichi 466-8555, Japan.
OptoBioTechnology Research Center, Nagoya Institute of Technology, Nagoya, Aichi 466-8555, Japan.

Hideki Kandori (H)

Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Nagoya, Aichi 466-8555, Japan.
OptoBioTechnology Research Center, Nagoya Institute of Technology, Nagoya, Aichi 466-8555, Japan.

Classifications MeSH