Calcium Binding to TAT Rhodopsin.


Journal

The journal of physical chemistry. B
ISSN: 1520-5207
Titre abrégé: J Phys Chem B
Pays: United States
ID NLM: 101157530

Informations de publication

Date de publication:
24 03 2022
Historique:
pubmed: 10 3 2022
medline: 23 4 2022
entrez: 9 3 2022
Statut: ppublish

Résumé

Rhodopsin is a large family of retinal-binding photoreceptive proteins found in animals and microbes. The retinal chromophore is normally positively charged by protonation of the Schiff base linkage, which is stabilized by the negatively charged counterion(s) such as aspartates, glutamates, and chloride ions. In contrast, no cation binding was reported near the retinal chromophore under physiological pH, presumably because of the electrostatic repulsion. Sodium binding takes place in light-driven sodium pumps, but the binding near the retinal chromophore is a transient event. Here, we report Ca

Identifiants

pubmed: 35262367
doi: 10.1021/acs.jpcb.2c00233
doi:

Substances chimiques

Schiff Bases 0
Rhodopsin 9009-81-8
Sodium 9NEZ333N27
Calcium SY7Q814VUP

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

2203-2207

Auteurs

Teppei Sugimoto (T)

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

Kota Katayama (K)

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

Hideki Kandori (H)

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

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Classifications MeSH