Fluorescence of blowfly metarhodopsin
نویسندگان
چکیده
منابع مشابه
Photosensitivity spectrum of crayfish rhodopsin measured using fluorescence of metarhodopsin
Discrepancies exist among spectral measurements of sensitivity of crayfish photoreceptors, their absorption in situ, and the number and absorption spectra of crayfish photopigments that are extracted by digitonin solutions. We have determined the photosensitivity spectrum of crayfish rhodopsin in isolated rhabdoms using long wavelength fluorescence emission from crayfish metarhodopsin as an int...
متن کاملTautomeric Forms of Metarhodopsin
Light isomerizes the chromophore of rhodopsin, 11-cis retinal (formerly retinene), to the all-trans configuration. This introduces a succession of unstable intermediates-pre-lumirhodopsin, lumirhodopsin, metarhodopsin -in which all-trans retinal is still attached to the chromophoric site on opsin. Finally, retinal is hydrolyzed from opsin. The present experiments show that metarhodopsin exists ...
متن کاملSignaling states of rhodopsin. Formation of the storage form, metarhodopsin III, from active metarhodopsin II.
Vertebrate rhodopsin consists of the apoprotein opsin and the chromophore 11-cis-retinal covalently linked via a protonated Schiff base. Upon photoisomerization of the chromophore to all-trans-retinal, the retinylidene linkage hydrolyzes, and all-trans-retinal dissociates from opsin. The pigment is eventually restored by recombining with enzymatically produced 11-cis-retinal. All-trans-retinal ...
متن کاملHydrogen bonding changes of internal water molecules in rhodopsin during metarhodopsin I and metarhodopsin II formation.
Rhodopsin is a 7-helix, integral membrane protein found in the rod outer segments, which serves as the light receptor in vision. Light absorption by the retinylidene chromophore of rhodopsin triggers an 11-cis-->all-trans isomerization, followed by a series of protein conformational changes, which culminate in the binding and activation of the G-protein transducin by the metarhodopsin II (Meta ...
متن کاملTemperature and pH dependence of the metarhodopsin I-metarhodopsin II equilibrium and the binding of metarhodopsin II to G protein in rod disk membranes
The equilibria between metarhodopsins I and II (MI and MII) and the binding of MII to retinal G protein (G) were investigated, using the dual wavelength absorbance response of rod disk membrane (RDM) suspensions to a series of small bleaches, together with a nonlinear least-squares fitting procedure that decouples the two reactions. This method has been subjected to a variety of theoretical and...
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ژورنال
عنوان ژورنال: Biophysics of Structure and Mechanism
سال: 1983
ISSN: 0340-1057,1432-1017
DOI: 10.1007/bf00535666