ArticleBiophysical journal2013
Large deformation of helix F during the photoreaction cycle of Pharaonis halorhodopsin in complex with azide.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 28 citations in OpenAlex.
- Structural insights into light-driven anion pumping in cyanobacteria.Nature communications · 2022Article
- Pumping mechanism of NM-R3, a light-driven bacterial chloride importer in the rhodopsin family.Science advances · 2020Article
- Effect of a bound anion on the structure and dynamics of halorhodopsin fromStructural dynamics (Melville, N.Y.) · 2019Article
- Toward the Optical Cochlear Implant.Cold Spring Harbor perspectives in medicine · 2019Review
- High frequency neural spiking and auditory signaling by ultrafast red-shifted optogenetics.Nature communications · 2018Article
- A Unique Light-Driven Proton Transportation Signal in Halorhodopsin from Natronomonas pharaonis.Biophysical journal · 2016Article
- Crystal structure of Halobacterium salinarum halorhodopsin with a partially depopulated primary chloride-binding site.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Eukaryotic G protein-coupled receptors as descendants of prokaryotic sodium-translocating rhodopsins.Biology direct · 2015Article
- Crystal structures of the L1, L2, N, and O states of pharaonis halorhodopsin.Biophysical journal · 2015Article
- Electrostatic interactions and hydrogen bond dynamics in chloride pumping by halorhodopsin.Biochimica et biophysica acta · 2014Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Halorhodopsin from Natronomonas pharaonis (pHR), a retinylidene protein that functions as a light-driven chloride ion pump, is converted into a proton pump in the presence of azide ion. To clarify this conversion, we investigated light-induced structural changes in pHR using a C2 crystal that was prepared in the presence of Cl(-) and subsequently soaked in a solution containing azide ion. When the pHR-azide complex was illuminated at pH 9, a profound outward movement (∼4 Å) of the cytoplasmic half of helix F was observed in a subunit with the EF loop facing an open space. This movement created a long water channel between the retinal Schiff base and the cytoplasmic surface, along which a proton could be transported. Meanwhile, the middle moiety of helix C moved inward, leading to shrinkage of the primary anion-binding site (site I), and the azide molecule in site I was expelled out to the extracellular medium. The results suggest that the cytoplasmic half of helix F and the middle moiety of helix C act as different types of valves for active proton transport.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.