Modulation of photophysical properties of FAD by modications of the C-terminus of a ferrodoxin/flavodoxin reductase

VALLE, LORENA; ABATEDAGA, INÉS; MORÁN-VIEYRA, FAUSTINO E.; BORTOLOTTI, ANA; CORTEZ, NÉSTOR; BORSARELLI, CLAUDIO

Córdoba

Workshop; Procesos Fotoinducidos en Proteínas; 2013

Grupo Argentino de Fotobiología

The photosynthetic bacterium Rhodobacter capsulatus contains a single (flavodoxin)-NADP(H) oxido-reductase (RcFPR) that catalyzes electron transfer from NADP(H) to the flavodoxin nifF for nitrogenase reduction. The X-ray crystallography of the enzyme showed two domains harboring the FAD and NADP(H). A site-directed mutagenesis approach on RcFPR C-terminus was performed, producing three different mutants: A266Y, A266delta and A266Ydelta, (with delta = - FVGEGI) which modifies both structural and catalytic properties. In this work, we analyze the effect of the C-terminus mutagenesis on the FAD photophysical properties.