Characterization of iron binding to frataxin from Psychromonas ingrahamii

RIGAL JUAN B.; NOGUERA MARTIN E.; SANTOS JAVIER; ROMAN ERNESTO A.

Congreso; XLII Reunión Anual de la Sociedad Argentina de Biofísica; 2013

Frataxin is a protein highly conserved protein among biology kingdoms. In humans its absence yields Friedreich's ataxia. Its biological function is to bind and deliver iron to other protein partners. In our laboratory we study iron binding and its effect on stability and dynamics of different frataxin variants. In this work, we characterized iron binding to frataxin from Psychromonas ingrahamii at different metal and protein concentrations. The resulting binding isotherm will define the metal affinity and stoichiometry to this protein. Previous results reported for other frataxin variants suggest that metal binding could move protein equilibrium towards oligomeric species1. This fact will be studied by light scattering and native gel techniques.