RT Journal Article
T1 Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach
A1 Simón Vázquez, Rosana
A1 Dominguez Seoane, Marta
A1 Lórenz Fonfría, Víctor A.
A1 Álvarez Rodríguez, Susana
A1 Bourdelande, José Luís
A1 Rodríguez de Lera, Ángel
A1 Padrós, Esteve
A1 Perálvarez Marín, Alex
K1 2406 Biofísica
AB Bacteriorhodopsin has a polar cluster of amino acids surrounding the retinal molecule, which is responsible for light harvesting to fuel proton pumping. From our previous studies, we have shown that threonine 90 is the pivotal amino acid in this polar cluster, both functionally and structurally. In an attempt to perform a phenotype rescue, we have chemically designed a retinal analogue molecule to compensate the drastic effects of the T90A mutation in bacteriorhodopsin. This analogue substitutes the methyl group at position C13 of the retinal hydrocarbon chain by and ethyl group (20-methyl retinal). We have analyzed the effect of reconstituting the wild-type and the T90A mutant apoproteins with all-trans-retinal and its 20-methyl derivative (hereafter, 13-ethyl retinal). Biophysical characterization indicates that recovering the steric interaction between the residue 90 and retinal, eases the accommodation of the chromophore, however it is not enough for a complete phenotype rescue. The characterization of these chemically engineered chromoproteins provides further insight into the role of the hydrogen bond network and the steric interactions involving the retinal binding pocket inbacteriorhodopsin and other microbial sensory rhodopsins.
PB PLoS ONE
SN 19326203
YR 2012
FD 2012-08-03
LK http://hdl.handle.net/11093/8124
UL http://hdl.handle.net/11093/8124
LA eng
NO PLoS ONE, 7(8): e42447 (2012)
NO Ministerio de Ciencia e Innovación | Ref. BES-2004-5542
DS Investigo
RD 15-mar-2025