Single molecule kinetics of bacteriorhodopsin by HS-AFM.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
10 12 2021
10 12 2021
Historique:
received:
26
07
2021
accepted:
30
11
2021
entrez:
11
12
2021
pubmed:
12
12
2021
medline:
11
1
2022
Statut:
epublish
Résumé
Bacteriorhodopsin is a seven-helix light-driven proton-pump that was structurally and functionally extensively studied. Despite a wealth of data, the single molecule kinetics of the reaction cycle remain unknown. Here, we use high-speed atomic force microscopy methods to characterize the single molecule kinetics of wild-type bR exposed to continuous light and short pulses. Monitoring bR conformational changes with millisecond temporal resolution, we determine that the cytoplasmic gate opens 2.9 ms after photon absorption, and stays open for proton capture for 13.2 ms. Surprisingly, a previously active protomer cannot be reactivated for another 37.6 ms, even under excess continuous light, giving a single molecule reaction cycle of ~20 s
Identifiants
pubmed: 34893646
doi: 10.1038/s41467-021-27580-2
pii: 10.1038/s41467-021-27580-2
pmc: PMC8664958
doi:
Substances chimiques
Proton Pumps
0
Receptors, Opioid
0
Bacteriorhodopsins
53026-44-1
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
7225Subventions
Organisme : NCCIH NIH HHS
ID : DP1 AT010874
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS110790
Pays : United States
Informations de copyright
© 2021. The Author(s).
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