ArticleBiophysical journal1994
Photoactivation of rhodopsin involves alterations in cysteine side chains: detection of an S-H band in the Meta I-->Meta II FTIR difference spectrum.
Article in Biophysical journal, 1994. 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.
- Nanosecond Transient IR Spectroscopy of Halorhodopsin in Living Cells.Journal of the American Chemical Society · 2024Article
- Dynamics of the Second Extracellular Loop Control Transducer Coupling of Peptide-Activated GPCRs.International journal of molecular sciences · 2023Article
- Comparison of the structural changes occurring during the primary phototransition of two different channelrhodopsins from Chlamydomonas algae.Biochemistry · 2015Article
- Intramolecular interactions that induce helical rearrangement upon rhodopsin activation: light-induced structural changes in metarhodopsin IIa probed by cysteine S-H stretching vibrations.The Journal of biological chemistry · 2014Article
- Mapping of the local environmental changes in proteins by cysteine scanning.Biophysics (Nagoya-shi, Japan) · 2014Article
- Vibrational spectroscopy of an algal Phot-LOV1 domain probes the molecular changes associated with blue-light reception.Biophysical journal · 2003Article
- The protein environment surrounding tyrosyl radicals D. and Z. in photosystem II: a difference Fourier-transform infrared spectroscopic study.Biophysical journal · 1998Article
- Hydrogen bonding changes of internal water molecules in rhodopsin during metarhodopsin I and metarhodopsin II formation.The Biochemical journal · 1998Article
- Photoactivation of rhodopsin causes an increased hydrogen-deuterium exchange of buried peptide groups.Biophysical journal · 1998Article
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Authors and funding
4 authors.
Funding
Abstract
FTIR difference spectroscopy has been used to study the role of cysteine residues in the photoactivation of rhodopsin. A positive band near 2550 cm-1 with a low frequency shoulder is detected during rhodopsin photobleaching, which is assigned on the basis of its frequency and isotope shift to the S-H stretching mode of one or more cysteine residues. Time-resolved studies at low temperature show that the intensity of this band correlates with the formation and decay kinetics of the Meta II intermediate. Modification of rhodopsin with the reagent NEM, which selectively reacts with the SH groups of Cys-140 and Cys-316 on the cytoplasmic surface of rhodopsin, has no effect on the appearance of this band. Four other cysteine residues are also unlikely to contribute to this band because they are either thio-palmitylated (Cys-322 and Cys-323) or form a disulfide bond (Cys-110 and Cys-187). On this basis, it is likely that at least one of the four remaining cysteine residues in rhodopsin is structurally active during rhodopsin photoactivation. The possibility is also considered that this band arises from a transient cleavage of the disulfide bond between cysteine residues 110 and 187.
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