ArticleBiophysical journal2001
Static and time-resolved step-scan Fourier transform infrared investigations of the photoreaction of halorhodopsin from Natronobacterium pharaonis: consequences for models of the anion translocation mechanism.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 62 citations in OpenAlex.
- Nanosecond Transient IR Spectroscopy of Halorhodopsin in Living Cells.Journal of the American Chemical Society · 2024Article
- Diversity, Mechanism, and Optogenetic Application of Light-Driven Ion Pump Rhodopsins.Advances in experimental medicine and biology · 2021Review
- Crystal structures of the L1, L2, N, and O states of pharaonis halorhodopsin.Biophysical journal · 2015Article
- Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.Chemical reviews · 2014Review
- Transient protonation changes in channelrhodopsin-2 and their relevance to channel gating.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Homotrimer formation and dissociation of pharaonis halorhodopsin in detergent system.Biophysical journal · 2012Article
- A gene-fusion strategy for stoichiometric and co-localized expression of light-gated membrane proteins.Nature methods · 2011Article
- Characterization of the primary photochemistry of proteorhodopsin with femtosecond spectroscopy.Biophysical journal · 2008Article
- The nitrate transporting photochemical reaction cycle of the pharaonis halorhodopsin.Biophysical journal · 2004Article
- Time-resolved FTIR studies of sensory rhodopsin II (NpSRII) from Natronobacterium pharaonis: implications for proton transport and receptor activation.Biophysical journal · 2003Article
- Temperature and halide dependence of the photocycle of halorhodopsin from Natronobacterium pharaonis.Biophysical journal · 2001Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
The molecular changes during the photoreaction of halorhodopsin from Natronobacterium pharaonis have been monitored by low-temperature static and by time-resolved step-scan Fourier transform infrared difference spectroscopy. In the low-temperature L spectrum anions only influence a band around 1650 cm(-1), tentatively assigned to the C=N stretch of the protonated Schiff base of L. The analysis of the time-resolved spectra allows to identify the four states: K, L(1), L(2), and O. Between L(1) and L(2), only the apoprotein undergoes alterations. The O state is characterized by an all-trans chromophore and by rather large amide I spectral changes. Because in our analysis the intermediate containing O is in equilibrium with a state indistinguishable from L(2), we are unable to identify an N-like state. At very high chloride concentrations (>5 M), we observe a branching of the photocycle from L(2) directly back to the dark state, and we provide evidence for direct back-isomerization from L(2). This branching leads to the reported reduction of transport activity at such high chloride concentrations. We interpret the L(1) to L(2) transition as an accessibility change of the anion from the extracellular to the cytosolic side, and the large amide I bands in O as an indication for opening of the cytosolic channel from the Schiff base toward the cytosolic surface and/or as indication for changes of the binding constant of the release site.
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