Aware of the importance of electrostatic and hydrophobic interactions in the formation of complexes that allow an efficient electron transfer between
molecules, such as the ferredoxin NADP + reeducates (FNR) and ferredoxin (Fd). The FNR catalyzes the transfer of electrons sequentially from two molecules of Fd to NADP + molecule in order to store energy in the form of reducing power NADPH.

We have seen that certain residues in the FNR are also critical for interaction with flavodoxin (Fled), redo protein binding of flaying mononucleotide, though,
so far, has not found any clue to her that waste may be associated with side
chains of FNR.

This collaboration between the Faculty of Sciences of the University of Zaragoza and a joint center at the University of Seville and the CSIC seeks to identify the structures involved in these interactions responsible for electron transfer between redo proteins and the enzyme responsible for its catalysis.

To do this, have modified individual side chains of residues E16, E20, E61, D65 and D96 Fled surface, either by introducing positive charges or neutralized. The results indicate that lthough these negative side chains contribute to the orientation and ptimization of the interaction of Fled to FNR or photo ystem I
(PSI) (responsible for the photo reduction of oxidized flavodoxin), none of them is involved in optimal interaction with the FNR. With these data in hand, the authors suggest that the interaction between FNR and Fled is less specific than that between FNR and Fd, and shed light on the role played by these and other residues in electron transfer and interaction with the enzymes esponsible.