ArticleProceedings of the National Academy of Sciences of the United States of America1994
Removal of transducer HtrI allows electrogenic proton translocation by sensory rhodopsin I.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 102 citations in OpenAlex.
- Earliest Photic Zone Niches Probed by Ancestral Microbial Rhodopsins.Molecular biology and evolution · 2022Article
- Conversion of microbial rhodopsins: insights into functionally essential elements and rational protein engineering.Biophysical reviews · 2017Review
- Microbial rhodopsins: wide distribution, rich diversity and great potential.Biophysics and physicobiology · 2015Review
- Mechanism divergence in microbial rhodopsins.Biochimica et biophysica acta · 2014Review
- Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.Chemical reviews · 2014Review
- Opposite displacement of helix F in attractant and repellent signaling by sensory rhodopsin-Htr complexes.The Journal of biological chemistry · 2011Article
- Sensory rhodopsin-I as a bidirectional switch: opposite conformational changes from the same photoisomerization.Biophysical journal · 2011Article
- A microbial rhodopsin with a unique retinal composition shows both sensory rhodopsin II and bacteriorhodopsin-like properties.The Journal of biological chemistry · 2011Article
- An inward proton transport using Anabaena sensory rhodopsin.Journal of microbiology (Seoul, Korea) · 2011Review
- Attractant and repellent signaling conformers of sensory rhodopsin-transducer complexes.Biochemistry · 2010Article
- Protein-protein interaction changes in an archaeal light-signal transduction.Journal of biomedicine & biotechnology · 2010Article
- A Schiff base connectivity switch in sensory rhodopsin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Different dark conformations function in color-sensitive photosignaling by the sensory rhodopsin I-HtrI complex.Biophysical journal · 2007Article
- Three strategically placed hydrogen-bonding residues convert a proton pump into a sensory receptor.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Time-resolved detection of sensory rhodopsin II-transducer interaction.Biophysical journal · 2004Article
- Light-induced behavioral responses (;phototaxis') in prokaryotes.Photosynthesis research · 2003Article
- Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction.Science (New York, N.Y.) · 2001Article
- Electrophysiological characterization of specific interactions between bacterial sensory rhodopsins and their transducers.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Photo-induced proton transport of pharaonis phoborhodopsin (sensory rhodopsin II) is ceased by association with the transducer.Biophysical journal · 2001Article
- Multicolored protein conformation states in the photocycle of transducer-free sensory rhodopsin-I.Biophysical journal · 2001Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Sensory rhodopsin I (sR-I) is a phototaxis receptor in halobacteria, which is closely related to the light-driven proton pump bacteriorhodopsin and the chloride pump halorhodopsin found in the same organisms. The three pigments undergo similar cyclic photoreactions, in spite of their different functions. In intact cells or isolated membranes sR-I is complexed with protein HtrI, the next link in the signal transduction chain, and does not function as an electrogenic ion pump. However, illumination of sR-I in membranes lacking HtrI causes pH changes in the medium, and its photoreaction kinetics become pH-dependent. We show here that in closed vesicles, near neutral pH it functions as an electrogenic proton pump capable of generating at least -80 mV transmembrane potential. The action spectrum shows a maximum 37 nm below the 587-nm absorption maximum of the native pigment. This apparent discrepancy occurs because the 587-nm form of HtrI-free sR-I exists in a pH-dependent equilibrium with a 550-nm absorbing species generated through deprotonation of one group with a pKa of 7.2, which we have tentatively identified as Asp-76. We interpret the results in terms of a general model for ion translocation by the bacterial rhodopsins.
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