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
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