![]() Dick, A search for radical intermediates in the photocycle of LOV domains, Photochem. Getzoff, Structural tuning of the fluorescent protein iLOV for improved photostability, J. Christie, The photoreversible fluorescent protein iLOV outperforms GFP as a reporter of plant virus infection, Proc. Ketley, Lighting up my life: a LOV-based fluorescent reporter for Campylobacter jejuni, Res. Yun, Engineering an FMN-based iLOV protein for the detection of arsenic ions, Anal. Möglich, Blue-Light Receptors for Optogenetics, Chem. Newly suggested FbFPs can be used for multicolor imaging and also as components of FRET pairs.Ī. Substitution with 1-deaza-FMN and the point mutations of the apoprotein result in a set of novel fluorescent proteins with emission bands in the “transparent” window where light readily penetrates through mammalian tissues. We found that point mutations of the apoprotein and substitution of FMN with either 8-amino-FMN or 8-methylamino-FMN lead to the red shift of emission bands up to 100 nm. We report the results of computational studies of iLOV variants, introducing point mutations and chromophore analogues. Therefore the upcoming challenge is to introduce novel variants of FbFPs to extend their color palette. The main limitation of FbFPs is that all the members have close values of their absorption and emission band maxima. It is becoming a popular tool for bioanalytical applications and bioimaging as a competitor of the well-known green fluorescent protein and its analogues. The iLOV protein is a promising member of the class of flavin mononucleotide (FMN) based fluorescent proteins (FbFPs).
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