ArticleBiophysical journal1998
Photoactivation of rhodopsin causes an increased hydrogen-deuterium exchange of buried peptide groups.
Article in Biophysical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Hydration-mediated G-protein-coupled receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A large geometric distortion in the first photointermediate of rhodopsin, determined by double-quantum solid-state NMR.Journal of biomolecular NMR · 2012Article
- Role of bulk water in hydrolysis of the rhodopsin chromophore.The Journal of biological chemistry · 2011Article
- Conserved waters mediate structural and functional activation of family A (rhodopsin-like) G protein-coupled receptors.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Internal hydration increases during activation of the G-protein-coupled receptor rhodopsin.Journal of molecular biology · 2008Article
- Perturbations at the chloride site during the photosynthetic oxygen-evolving cycle.Photosynthesis research · 2007Article
- FTIR difference spectroscopy in combination with isotope labeling for identification of the carbonyl modes of P700 and P700+ in photosystem I.Biophysical journal · 2004Article
- Photo-oxidation of P740, the primary electron donor in photosystem I from Acaryochloris marina.Biophysical journal · 2003Article
- G protein-coupled receptor rhodopsin: a prospectus.Annual review of physiology · 2003Review
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Authors and funding
3 authors.
Funding
Abstract
A key step in visual transduction is the light-induced conformational changes of rhodopsin that lead to binding and activation of the G-protein transducin. In order to explore the nature of these conformational changes, time-resolved Fourier transform infrared spectroscopy was used to measure the kinetics of hydrogen/deuterium exchange in rhodopsin upon photoexcitation. The extent of hydrogen/deuterium exchange of backbone peptide groups can be monitored by measuring the integrated intensity of the amide II and amide II' bands. When rhodopsin films are exposed to D2O in the dark for long periods, the amide II band retains at least 60% of its integrated intensity, reflecting a core of backbone peptide groups that are resistant to H/D exchange. Upon photoactivation, rhodopsin in the presence of D2O exhibits a new phase of H/D exchange which at 10 degrees C consists of fast (time constant approximately 30 min) and slow (approximately 11 h) components. These results indicate that photoactivation causes buried portions of the rhodopsin backbone structure to become more accessible.
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