The uncoupling of bacteriorhodopsin by high temperature and anaesthetics
Abstract
1. General anaesthetics induce reversible structural and functional modifications of the proton pump bacteriorhodopsin contained in the purple membrane of halobacteria. 2. This short paper describes the phenomenological similarity between the effects of anaesthetics and heating on this system. 3. pH dependence and thermal analysis suggest that the structural change taking place at room temperature in the presence of anaesthetic is the same as that observed at temperatures higher than 70 degrees C in the native membrane. In addition, part of the structural modification has an irreversible character when induced by anaesthetic as well as by heating.
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Volatile anesthetics act on species across the evolutionary tree, not only on human patients.
“However, volatile anesthetics exert actions not only on human patients, but on species spanning the evolutionary tree of life [1–8] (Figure 1).”
From The Biology of General Anesthesia from Paramecium to Primate (2019) · cites this paper as [4]
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References 13 · Cited by 5
- Authors
- Gao, M. M., & Boucher, F.
- Affiliations
- Université du Québec à Trois-Rivières (CA)
- Corresponding author
- Gao, Méi Méi
- Venue
- Toxicology Letters
- Publisher
- Elsevier BV
- Published
- 1998-11
- Volume
- 100-101
- Pages
- 393-396
- ISSN
- 0378-4274 (ISSN-L)
- OpenAlex
- W2051455708
- Cited by
- 5
- References
- 13
- Citations by year
- 2019: 1 · 2013: 1
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Toxicology Letters (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- bacteriorhodopsin, general anesthetics, high temperature, purple membrane, halobacteria, proton pump, protein conformational change, pH dependence, thermal analysis
- MeSH terms
- Anesthetics, Bacteriorhodopsins, Calorimetry, Differential Scanning, Hot Temperature, Hydrogen-Ion Concentration, Photochemistry, Spectrophotometry, Infrared, Temperature, Xenobiotics
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