ArticleThe Journal of biological chemistry2009
His-75 in proteorhodopsin, a novel component in light-driven proton translocation by primary pumps.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 75 citations in OpenAlex.
- Proteorhodopsin insights into the molecular mechanism of vectorial proton transport.Science advances · 2025Article
- A Proteorhodopsin-Related Photosensor Expands the Repertoire of Structural Motifs Employed by Sensory Rhodopsins.The journal of physical chemistry. B · 2023Article
- Expression of Xanthorhodopsin in Escherichia coli.The protein journal · 2023Article
- Structural and functional consequences of the H180A mutation of the light-driven sodium pump KR2.Biophysical journal · 2023Article
- Probing Channelrhodopsin Electrical Activity in Algal Cell Populations.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Role of Thr82 for the unique photochemistry of TAT rhodopsin.Biophysics and physicobiology · 2021Article
- Diversity, Mechanism, and Optogenetic Application of Light-Driven Ion Pump Rhodopsins.Advances in experimental medicine and biology · 2021Review
- Functional importance of the oligomer formation of the cyanobacterial HScientific reports · 2019Article
- Photocycle-dependent conformational changes in the proteorhodopsin cross-protomer Asp-His-Trp triad revealed by DNP-enhanced MAS-NMR.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Raman spectroscopy of a near infrared absorbing proteorhodopsin: Similarities to the bacteriorhodopsin O photointermediate.PloS one · 2018Article
- Structural Changes in an Anion Channelrhodopsin: Formation of the K and L Intermediates at 80 K.Biochemistry · 2017Article
- X-ray Crystallographic Structure of Thermophilic Rhodopsin: IMPLICATIONS FOR HIGH THERMAL STABILITY AND OPTOGENETIC FUNCTION.The Journal of biological chemistry · 2016Article
- Assembling a Correctly Folded and Functional Heptahelical Membrane Protein by Protein Trans-splicing.The Journal of biological chemistry · 2015Article
- Functional consequences of the oligomeric assembly of proteorhodopsin.Journal of molecular biology · 2015Article
- His166 is the Schiff base proton acceptor in attractant phototaxis receptor sensory rhodopsin I.Biochemistry · 2014Article
- Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.Chemical reviews · 2014Review
- Gloeobacter rhodopsin, limitation of proton pumping at high electrochemical load.Biophysical journal · 2013Article
- Lipid bilayer composition can influence the orientation of proteorhodopsin in artificial membranes.Biophysical journal · 2013Article
- Thermal and spectroscopic characterization of a proton pumping rhodopsin from an extreme thermophile.The Journal of biological chemistry · 2013Article
- Breaking the carboxyl rule: lysine 96 facilitates reprotonation of the Schiff base in the photocycle of a retinal protein from Exiguobacterium sibiricum.The Journal of biological chemistry · 2013Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Proteorhodopsins (PRs), photoactive retinylidene membrane proteins ubiquitous in marine eubacteria, exhibit light-driven proton transport activity similar to that of the well studied bacteriorhodopsin from halophilic archaea. However, unlike bacteriorhodopsin, PRs have a single highly conserved histidine located near the photoactive site of the protein. Time-resolved Fourier transform IR difference spectroscopy combined with visible absorption spectroscopy, isotope labeling, and electrical measurements of light-induced charge movements reveal participation of His-75 in the proton translocation mechanism of PR. Substitution of His-75 with Ala or Glu perturbed the structure of the photoactive site and resulted in significantly shifted visible absorption spectra. In contrast, His-75 substitution with a positively charged Arg did not shift the visible absorption spectrum of PR. The mutation to Arg also blocks the light-induced proton transfer from the Schiff base to its counterion Asp-97 during the photocycle and the acid-induced protonation of Asp-97 in the dark state of the protein. Isotope labeling of histidine revealed that His-75 undergoes deprotonation during the photocycle in the proton-pumping (high pH) form of PR, a reaction further supported by results from H75E. Finally, all His-75 mutations greatly affect charge movements within the PR and shift its pH dependence to acidic values. A model of the proteorhodopsin proton transport process is proposed as follows: (i) in the dark state His-75 is positively charged (protonated) over a wide pH range and interacts directly with the Schiff base counterion Asp-97; and (ii) photoisomerization-induced transfer of the Schiff base proton to the Asp-97 counterion disrupts its interaction with His-75 and triggers a histidine deprotonation.
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