ROLE OF ANABAENA FLAVODOXIN HYDROPHOBIC RESIDUES IN PROTEIN-PROTEIN INTERACTION AND ELECTRON TRANSFER TO FERREDOXIN-NADP~+ REDUCTASE

摘要

Biochemical and structural studies indicate that electrostatic and hydrophobic interactions play an important role in formation of optimal complexes for efficient electron transfer between ferredoxin-NADP~+ reductase (FNR) and ferredoxin (Fd) (Medinaet al 2004), Moreover, it has been shown that several charged and hydrophobic residues on the FNR surface are also critical for the interaction with flavodoxin (Fld) (Medina et al 2004), although, so far, no key residue on the Fld surface has been foundto be the counterpart of FNR side-chains (Casaus et al 2002, Nogues et al 2003).