ArticleThe journal of physical chemistry. B2025
Combined Mutational and Spectroscopic Study on the Calcium-Related Kinetic Effects on the VirChR1 Photocycle.
Article in The journal of physical chemistry. B, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Molecular mechanism of calcium inhibition in viral channelrhodopsins.Nature communications · 2026Article
- FTIR study of the wild-type and mutant proteins of a viral rhodopsin, OLPVR1.Biophysics and physicobiology · 2025Article
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Authors and funding
5 authors.
Funding
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Abstract
The viral rhodopsin 1 subfamily consists of microbial rhodopsins, such as VirChR1, with a light-gated cation channeling functionality, which is inhibited by calcium. For VirChR1, S14, E54, and N225 have been proposed as key residues for calcium binding. They form a highly conserved SEN-triad in channelrhodopsins near the functionally important central gate. Here, we present a time-resolved UV/vis spectroscopic study on the VirChR1 variants S14A, E54A, and N225A in a calcium-dependent manner. Comparison with the calcium-associated effects observed for the wild type shed light on the role of the respective residues for the calcium interaction. While S14A shows less pronounced, yet similar, signals, indicative of a reduced calcium affinity, E54A exhibits nearly calcium-independent photocycle kinetics, highlighting its crucial role for calcium binding. The N225A variant shows altered photocycle kinetics, in both the absence and presence of calcium, demonstrating its critical role in the formation of the functionally important central gate in VirChR1.
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