ArticleBiophysical journal2003
Characterization of the photochemical reaction cycle of proteorhodopsin.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Diverging pH dependence and photocycle dynamics across members of the CryoRhodopsin clade.Biophysical journal · 2026Article
- CryoRhodopsins: A comprehensive characterization of a group of microbial rhodopsins from cold environments.Science advances · 2025Article
- A Detailed View on the (Re)isomerization Dynamics in Microbial Rhodopsins Using Complementary Near-UV and IR Readouts.Angewandte Chemie (International ed. in English) · 2025Article
- Long-Time Scale Simulations Reveal Key Dynamics That Drive the Onset of the N State in the Proteorhodopsin Photocycle.The journal of physical chemistry. B · 2024Article
- Lipid membrane mimetics and oligomerization tune functional properties of proteorhodopsin.Biophysical journal · 2023Article
- From the Sea for the Sight: Marine Derived Products for Human Vision.Frontiers in aging neuroscience · 2022Review
- Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Temperature Dependence of the Krokinobacter rhodopsin 2 Kinetics.Biophysical journal · 2021Article
- Lokiarchaeota archaeon schizorhodopsin-2 (LaSzR2) is an inward proton pump displaying a characteristic feature of acid-induced spectral blue-shift.Scientific reports · 2020Article
- Electrostatic Environment of Proteorhodopsin Affects the pKa of Its Buried Primary Proton Acceptor.Biophysical journal · 2020Article
- Cryo-electron microscopic and X-ray crystallographic analysis of the light-driven proton pump proteorhodopsin reveals a pentameric assembly.Journal of structural biology: X · 2020Article
- Photoreaction Dynamics of Red-Shifting Retinal Analogues Reconstituted in Proteorhodopsin.The journal of physical chemistry. B · 2019Article
- Strong pH-Dependent Near-Infrared Fluorescence in a Microbial Rhodopsin Reconstituted with a Red-Shifting Retinal Analogue.The journal of physical chemistry letters · 2018Article
- Allosteric Effects of the Proton Donor on the Microbial Proton Pump Proteorhodopsin.Biophysical journal · 2018Article
- Functionally Active Membrane Proteins Incorporated in Mesostructured Silica Films.Journal of the American Chemical Society · 2018Article
- Asymmetric Functional Conversion of Eubacterial Light-driven Ion Pumps.The Journal of biological chemistry · 2016Article
- Characterization of a Cyanobacterial Chloride-pumping Rhodopsin and Its Conversion into a Proton Pump.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
- Light-driven Na(+) pump from Gillisia limnaea: a high-affinity Na(+) binding site is formed transiently in the photocycle.Biochemistry · 2014Article
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Authors and funding
4 authors.
Funding
Abstract
Absorption changes in the photocycle of the recently described retinal protein, proteorhodopsin, are analyzed. The transient spectra at pH 9.5, where it acts as a light-driven proton pump, reveal the existence of three spectrally different intermediates, K, M, and N, named in analogy with the photointermediates of bacteriorhodopsin. Model analysis based on time-dependent absorption kinetic signals at four wavelengths suggested the existence of two more spectrally silent intermediates and lead to a sequential reaction scheme with five intermediates, K, M(1), M(2), N, and PR', before decay to the initial state PR. An L-like intermediate was not observed, probably for kinetic reasons. By measuring the light-generated electric signal of an oriented sample, the electrogenicity of each intermediate could be determined. The electrogenicities of the first three intermediates (K, M(1), and M(2)) have small negative value, but the last three components, corresponding to the N and PR' intermediates and PR, are positive and two-orders-of-magnitude larger. These states give the major contributions to the proton translocation across the membrane. The energetic scheme of the photocycle was calculated from the temperature-dependence of the absorption kinetic signals.
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