ArticleThe Journal of biological chemistry2015
Platymonas subcordiformis Channelrhodopsin-2 Function: I. THE PHOTOCHEMICAL REACTION CYCLE.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- A red-light gate for a cation channel: The conducting state of channelrhodopsin-1 from Chlamydomonas augustae.Biophysical journal · 2026Article
- Active and inactive pathways in the kinetic mechanism of the G51V retinitis pigmentosa mutant photoreaction.Biophysical journal · 2025Article
- Parallel photocycle kinetic model of anion channelrhodopsin GtACR1 function.Biophysical journal · 2024Article
- The open channel state in anion channelrhodopsin GtACR1 is a red-absorbing intermediate.Biophysical journal · 2024Article
- Isospectral intermediates in the photochemical reaction cycle of anion channelrhodopsin GtACR1.Biophysical journal · 2023Article
- Proton transfer reactions in the red light-activatable channelrhodopsin variant ReaChR and their relevance for its function.The Journal of biological chemistry · 2017Article
- Microbial Rhodopsins: Diversity, Mechanisms, and Optogenetic Applications.Annual review of biochemistry · 2017Review
- Complex Photochemistry within the Green-Absorbing Channelrhodopsin ReaChR.Biophysical journal · 2017Article
- Identification of a Natural Green Light Absorbing Chloride Conducting Channelrhodopsin from Proteomonas sulcata.The Journal of biological chemistry · 2016Article
- Platymonas subcordiformis Channelrhodopsin-2 (PsChR2) Function: II. RELATIONSHIP OF THE PHOTOCHEMICAL REACTION CYCLE TO CHANNEL CURRENTS.The Journal of biological chemistry · 2015Article
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Authors and funding
6 authors.
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Abstract
The photocycle kinetics of Platymonas subcordiformis channelrhodopsin-2 (PsChR2), among the most highly efficient light-gated cation channels and the most blue-shifted channelrhodopsin, was studied by time-resolved absorption spectroscopy in the 340-650-nm range and in the 100-ns to 3-s time window. Global exponential fitting of the time dependence of spectral changes revealed six lifetimes: 0.60 μs, 5.3 μs, 170 μs, 1.4 ms, 6.7 ms, and 1.4 s. The sequential intermediates derived for a single unidirectional cycle scheme based on these lifetimes were found to contain mixtures of K, L, M, O, and P molecular states, named in analogy to photointermediates in the bacteriorhodopsin photocycle. The photochemistry is described by the superposition of two independent parallel photocycles. The analysis revealed that 30% of the photoexcited receptor molecules followed Cycle 1 through the K, M, O, and P states, whereas 70% followed Cycle 2 through the K, L, M, and O states. The recovered state, R, is spectrally close, but not identical, to the dark state on the seconds time scale. The two-cycle model of this high efficiency channelrhodopsin-2 (ChR) opens new perspectives in understanding the mechanism of channelrhodopsin function.
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