Impact on the photophysical properties of cofactor FAD by C-terminus domain mutation in Rhodobacter capsulatus ferredoxin/flavodoxin NADP reductase

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

Cordoba

Conferencia; II Reunión de Fotobiólogos Moleculares Argentinos (II GRAFOB); 2013

"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 was performed, producing three different mutants: A266Y, A266 Δ and A266Y Δ, (with Δ = - FVGEGI) which modifies both structural and catalytic properties. In this work, the effect of the mutagenesis on the FAD photophysical properties of flavoenzime series was analyzed.