[Todos] seminario

[Enrique San Roman]

Hola a todos:

Tengo el placer de invitarlos al seminario que 
tendra lugar el viernes proximo en el horario 
habitrual de los Seinarios de Fotoquimica.

Saludos,
Enrique San Roman

Cristiano Viappani
e-mail: cristiano.viappiani en unipr.it

Dipartimento di Fisica e Scienze della Terra, 
Università di Parma, viale delle Scienze 7A, 43124, Parma, Italy

Viernes 4 de octubre, 10:00 hs., Aula Busch, Departamento de Quimica Inorganica


Photochromism in the bacterial photoreceptor YtvA 
is strongly affected by hydration

YtvA is a blue light photoreceptor from Bacillus 
subtilis, composed of a flavin-binding LOV- 
(light, oxygen, voltage) domain, sharing high 
structural homology with the flavin 
mononucleotide (FMN)-binding LOV domains of plant 
phototropins. When the fluorescent, dark adapted 
species (YtvAD) is illuminated with blue light, a 
photocycle is initiated, which proceeds through a 
triplet state leading in high yield to reversible 
formation of a non-fluorescent blue shifted 
FMN-cysteine C(4a)-thiol adduct (YtvAL). The 
photoadduct slowly reverts in the dark to the 
parent state YtvAD. The fluorescence emission by 
YtvAD offers a convenient means to follow the 
functional state of the molecule. We have 
recently shown that this fluorescent reporter has 
potential for super-resolution microscopy. YtvA 
is efficiently photo switchable between 
fluorescent and non fluorescent states using blue 
and violet light. We have exploited this property 
to perform sub-diffraction localization of 
individual YtvA molecules deposited on a 
coverslip and demonstrated Fluorescence 
PhotoActivation Localization Microscopy (FPALM) 
studies of live Escherichia coli cells, 
expressing YtvA molecules. Recent studies have 
suggested a strong influence of hydration on the 
dark relaxation rate from YtvAL to YtvAD, with 
remarkable implications for cellular applications.


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