Light-induced protein conformational changes in the photolysis of octopus rhodopsin.
AUTOR(ES)
Nakagawa, M
RESUMO
Light-induced protein conformational changes in the photolysis of octopus rhodopsin were measured with a highly sensitive time-resolved transient UV absorption spectrophotometer with nanosecond time resolution. A negative band around 280 nm in the lumirhodopsin minus rhodopsin spectra suggests that alteration of the environment of some of the tryptophan residues has taken place before the formation of lumirhodopsin. A small recovery of the absorbance at 280 nm was observed in the transformation of lumirhodopsin to mesorhodopsin. Kinetic parameters suggest that major conformational changes have taken place in the transformation of mesorhodopsin to acid metarhodopsin. In this transformation, drastic changes of amplitude and a shift of a difference absorption band around 280 nm take place, which suggest that some of the tryptophan residues of rhodopsin become exposed to a hydrophilic environment.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1184427Documentos Relacionados
- Light-induced currents in Xenopus oocytes expressing bovine rhodopsin.
- Light-induced Changes in Allophycocyanin 1
- Electron diffraction studies of light-induced conformational changes in the Leu-93 → Ala bacteriorhodopsin mutant
- Light-induced exposure of the cytoplasmic end of transmembrane helix seven in rhodopsin
- Abnormal photoresponses and light-induced apoptosis in rods lacking rhodopsin kinase