Sub-picosecond photo-isomerization is the major primary process of energy conversion in retinal proteins and has as such been in the focus of extensive theoretical and experimental work over the past decades. In this review article, we revisit the long-standing question as to how the protein tunes the isomerization speed and quantum yield. We focus on our recent contributions to this field, which underscore the concept of a delicate mixing of reactive and non-reactive excited states, as a result of steric properties and electrostatic interactions with the protein environment. Further avenues and new approaches are outlined which hold promise for advancing our understanding of these intimately coupled chromophore-protein systems
The photoisomerization of retinal in rhodopsin is modeled by a vibronically coupled electronic two-s...
none3siRetinal chromophores are the photoactive molecular units of visual and archaeal rhodopsins, a...
Proteorhodopsin (pR) is a membrane-embedded proton pump from the microbial rhodopsin family. Light a...
Sub-picosecond photo-isomerization is the major primary process of energy conversion in retinal prot...
The results of new and recently reported CASSCF/6-31G* photoisomerization path computations of a ser...
The visual pigment 11-cis-retinal is covalently bonded to Lys-296 of the heptahelical membrane prote...
Spectral data show that the photoisomerization of retinal protonated Schiff base (rPSB) chromophores...
The 13-cis to all-trans photoisomerisation of the retinal chromophore in bacteriorhodopsin (bR) is a...
Spectral data show that the photoisomerization of retinal protonated Schiff base (rPSB) chromophores...
Ultrafast processes in light-absorbing proteins have been implicated in the primary step in the ligh...
The photocycle of photoactive yellow protein (PYP) is initiated by a photoinduced trans–cis isomeriz...
A hallmark of the primary visual event is the barrierless, ultrafast, and efficient 11-cis to all-tr...
The photocycle of photoactive yellow protein (PYP) is initiated by a photoinduced trans-cis isomeris...
The photoisomerization of retinal in rhodopsin is modeled by a vibronically coupled electronic two-s...
none3siRetinal chromophores are the photoactive molecular units of visual and archaeal rhodopsins, a...
Proteorhodopsin (pR) is a membrane-embedded proton pump from the microbial rhodopsin family. Light a...
Sub-picosecond photo-isomerization is the major primary process of energy conversion in retinal prot...
The results of new and recently reported CASSCF/6-31G* photoisomerization path computations of a ser...
The visual pigment 11-cis-retinal is covalently bonded to Lys-296 of the heptahelical membrane prote...
Spectral data show that the photoisomerization of retinal protonated Schiff base (rPSB) chromophores...
The 13-cis to all-trans photoisomerisation of the retinal chromophore in bacteriorhodopsin (bR) is a...
Spectral data show that the photoisomerization of retinal protonated Schiff base (rPSB) chromophores...
Ultrafast processes in light-absorbing proteins have been implicated in the primary step in the ligh...
The photocycle of photoactive yellow protein (PYP) is initiated by a photoinduced trans–cis isomeriz...
A hallmark of the primary visual event is the barrierless, ultrafast, and efficient 11-cis to all-tr...
The photocycle of photoactive yellow protein (PYP) is initiated by a photoinduced trans-cis isomeris...
The photoisomerization of retinal in rhodopsin is modeled by a vibronically coupled electronic two-s...
none3siRetinal chromophores are the photoactive molecular units of visual and archaeal rhodopsins, a...
Proteorhodopsin (pR) is a membrane-embedded proton pump from the microbial rhodopsin family. Light a...