ArticleBiophysical journal2002
Energetics and volume changes of the intermediates in the photolysis of octopus rhodopsin at a physiological temperature.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 38 citations in OpenAlex.
- The Two-Photon Reversible Reaction of the Bistable Jumping Spider Rhodopsin-1.Biophysical journal · 2019Article
- Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.Chemical reviews · 2014Review
- Reaction dynamics of halorhodopsin studied by time-resolved diffusion.Biophysical journal · 2009Article
- Enthalpy changes during photosynthetic water oxidation tracked by time-resolved calorimetry using a photothermal beam deflection technique.Biophysical journal · 2008Article
- Photoreverse reaction dynamics of octopus rhodopsin.Biophysical journal · 2007Article
- Laser-induced transient grating analysis of dynamics of interaction between sensory rhodopsin II D75N and the HtrII transducer.Biophysical journal · 2007Article
- The A-Fx to F(A/B) step in synechocystis 6803 photosystem I is entropy driven.Journal of the American Chemical Society · 2006Article
- Time-resolved detection of sensory rhodopsin II-transducer interaction.Biophysical journal · 2004Article
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4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enthalpy changes (Delta H) of the photointermediates that appear in the photolysis of octopus rhodopsin were measured at physiological temperatures by the laser-induced transient grating method. The enthalpy from the initial state, rhodopsin, to bathorhodopsin, lumirhodopsin, mesorhodopsin, transient acid metarhodopsin, and acid metarhodopsin were 146 +/- 15 kJ/mol, 122 +/- 17 kJ/mol, 38 +/- 8 kJ/mol, 12 +/- 5 kJ/mol, and 12 +/- 5 kJ/mol, respectively. These values, except for lumirhodopsin, are similar to those obtained for the cryogenically trapped intermediate species by direct calorimetric measurements. However, the Delta H of lumirhodopsin at physiological temperatures is quite different from that at low temperature. The reaction volume changes of these processes were determined by the pulsed laser-induced photoacoustic method along with the above Delta H values. Initially, in the transformation between rhodopsin and bathorhodopsin, a large volume expansion of +32 +/- 3 ml/mol was obtained. The volume changes of the subsequent reaction steps were rather small. These results are compared with the structural changes of the chromophore, peptide backbone, and water molecules within the membrane helixes reported previously.
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