ArticleBiophysical journal2004
The assignment of the different infrared continuum absorbance changes observed in the 3000-1800-cm(-1) region during the bacteriorhodopsin photocycle.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 55 citations in OpenAlex.
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- Sul1 and Sul2 sulfate transceptors signal to protein kinase A upon exit of sulfur starvation.The Journal of biological chemistry · 2015Article
- Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle.Biophysical journal · 2012Article
- Infrared and visible absolute and difference spectra of bacteriorhodopsin photocycle intermediates.Applied spectroscopy · 2011Article
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- Identification of FTIR bands due to internal water molecules around the quinone binding sites in the reaction center from Rhodobacter sphaeroides.Biochemistry · 2009Article
- Monitoring light-induced structural changes of Channelrhodopsin-2 by UV-visible and Fourier transform infrared spectroscopy.The Journal of biological chemistry · 2008Article
- Structural changes due to the deprotonation of the proton release group in the M-photointermediate of bacteriorhodopsin as revealed by time-resolved FTIR spectroscopy.Biochemistry · 2008Article
- Structures and spectral signatures of protonated water networks in bacteriorhodopsin.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
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- Proton binding within a membrane protein by a protonated water cluster.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- A local area network of protonated water molecules.Biophysical journal · 2004Article
- A role for internal water molecules in proton affinity changes in the Schiff base and Asp85 for one-way proton transfer in bacteriorhodopsin.Photochemistry and photobiologyArticle
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4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bleach continuum in the 1900-1800-cm(-1) region was reported during the photocycle of bacteriorhodopsin (bR) and was assigned to the dissociation of a polarizable proton chain during the proton release step. More recently, a broad band pass filter was used and additional infrared continua have been reported: a bleach at >2700 cm(-1), a bleach in the 2500-2150-cm(-1) region, and an absorptive behavior in the 2100-1800-cm(-1) region. To fully understand the importance of the hydrogen-bonded chains in the mechanism of the proton transport in bR, a detailed study is carried out here. Comparisons are made between the time-resolved Fourier transform infrared spectroscopy experiments on wild-type bR and its E204Q mutant (which has no early proton release), and between the changes in the continua observed in thermally or photothermally heated water (using visible light-absorbing dye) and those observed during the photocycle. The results strongly suggest that, except for the weak bleach in the 1900-1800-cm(-1) region and >2500 cm(-1), there are other infrared continua observed during the bR photocycle, which are inseparable from the changes in the absorption of the solvent water molecules that are photothermally excited via the nonradiative relaxation of the photoexcited retinal chromophore. A possible structure of the hydrogen-bonded system, giving rise to the observed bleach in the 1900-1800-cm(-1) region and the role of the polarizable proton in the proton transport is discussed.
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