Photoactive proteins

On the ultrafast conversions from excited FC (Franck-Condon) state to FI (Fluorescence) state of chromophores in PNS of photoactive proteins PYP, Rh and FP... 

Figure 23-47 Ribbon drawing of the structure of the 125-residue yellow photoactive protein. The 4-hydroxycinnamoyl chromophore, which is attached to cysteine 69, is represented with balls and sticks. From Borgstahl et al.601 Courtesy of Gloria Borgstahl.

The importance of environmental effects on the processes at and near CIs is illustrated by recent experimental studies of biologically relevant systems, e.g. the chro-mophores of the rhodopsin family [10,11] and other photoactive proteins [12-16] as well as the building blocks of DNA [17,18] some solution studies have also been undertaken [89-91], These studies reveal the crucial role of CIs and suggest that a solvent or protein environment can have a pronounced impact on the electronic structure and Cl topology and the net rate of passage to the ground state. 

The reconstituted photoactive proteins may act as light-triggered cofactors, activating enzyme cascades. For example, the electron-transporting protein cytochrome... 

I Witt, HT Witt, S Gerken, W Saenger, JP Dekker and M R gner (1987) Crystallization of reaction center I of photosynthesis. Low-concentration crystallization of photoactive protein complexes from the cyanobacterium Synechococcus sp. FEBS Lett 221 260-264... 

Biotinylated copolymers of 3-undecylthiophene and 3-thienylmethanoI using streptavidin as a cross-linker protein is an electroactive matrix for the attachment of a photoactive protein, phycoerythrin. The biotinylation of the copolymer improves the film forming properties and results in a stable mono-layer. The phycoerythrin binding to the biotinylated copolymer monolayer can be monitored through fluorescence microscopy at the air-water interface [451]. 

Kubiak, K., 8c Nowak, W. (2008). Molecular dynamics simulations of the photoactive protein nitrile hydratase. Biophysical Journal, 94, 3824. 

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