The picosecond fluorescence kinetics and quantum yield from bovine rhodopsin were measured in the 5–40 degrees K range. The fluorescence rise and decay times are faster than our resolution of 15 ps (full width at half maximum) over this entire temperature range. The size of the observed emission was also temperature independent, and we find that the upper limit of rhodopsin's fluorescence quantum yield to be phi f approximately equal to 10(-5). Replacing all of rhodopsin's exchangeable protons with deuterons by suspending rhodopsin in D2O had no effect on either the kinetics of the emission or the value of the quantum yield. Our data provide strong confirmation of the idea that the first step in the visual process is an excited-state cis-to...
The excited state lifetime of bovine rhodopsin (Rh) increases from ca. 100 fs to 85 ps when the C11...
AbstractThe photoreaction quantum yield of rhodopsin is wavelength dependent: ϕ(λ) is reduced by up ...
The primary event in vision is induced by the ultrafast photoisomerization of rhodopsin, the dim-lig...
The picosecond fluorescence kinetics and quantum yield from bovine rhodopsin were measured in the 5–...
A synthetic retinal having a fixed 11-cis geometry has been used to prepare a nonbleachable analogue...
The fluorescence kinetics of bovine rhodopsin and isorhodopsin excited with a single picosecond lase...
Bovine rhodopsin and isorhodopsin were excited with a single 530-nm, 7-ps light pulse emitted by a m...
The excited state lifetime of bovine rhodopsin (Rh) increases from ca. 100 fs to 85 ps when the C11=...
The early events in halorhodopsin after light excitation are studied with picosecond time resolution...
The relative quantum yields of the photoreactions Rhodopsin in equilibrium Bathorhodopsin in equilib...
The early events in halorhodopsin after light excitation are studied with picosecond time resolution...
Data from picosecond spectroscopic studies of the formation kinetics of bathorhodopsin upon photolys...
The visual pigment 11-cis-retinal is covalently bonded to Lys-296 of the heptahelical membrane prote...
In our eyes light is absorbed by a polyene molecule called retinal. This molecule contains six doubl...
Ever since the conversion of the 11-cis retinal chromophore to its all-trans form in rhodopsin was i...
The excited state lifetime of bovine rhodopsin (Rh) increases from ca. 100 fs to 85 ps when the C11...
AbstractThe photoreaction quantum yield of rhodopsin is wavelength dependent: ϕ(λ) is reduced by up ...
The primary event in vision is induced by the ultrafast photoisomerization of rhodopsin, the dim-lig...
The picosecond fluorescence kinetics and quantum yield from bovine rhodopsin were measured in the 5–...
A synthetic retinal having a fixed 11-cis geometry has been used to prepare a nonbleachable analogue...
The fluorescence kinetics of bovine rhodopsin and isorhodopsin excited with a single picosecond lase...
Bovine rhodopsin and isorhodopsin were excited with a single 530-nm, 7-ps light pulse emitted by a m...
The excited state lifetime of bovine rhodopsin (Rh) increases from ca. 100 fs to 85 ps when the C11=...
The early events in halorhodopsin after light excitation are studied with picosecond time resolution...
The relative quantum yields of the photoreactions Rhodopsin in equilibrium Bathorhodopsin in equilib...
The early events in halorhodopsin after light excitation are studied with picosecond time resolution...
Data from picosecond spectroscopic studies of the formation kinetics of bathorhodopsin upon photolys...
The visual pigment 11-cis-retinal is covalently bonded to Lys-296 of the heptahelical membrane prote...
In our eyes light is absorbed by a polyene molecule called retinal. This molecule contains six doubl...
Ever since the conversion of the 11-cis retinal chromophore to its all-trans form in rhodopsin was i...
The excited state lifetime of bovine rhodopsin (Rh) increases from ca. 100 fs to 85 ps when the C11...
AbstractThe photoreaction quantum yield of rhodopsin is wavelength dependent: ϕ(λ) is reduced by up ...
The primary event in vision is induced by the ultrafast photoisomerization of rhodopsin, the dim-lig...