Nonheme iron protein isolated from lupine (Lupinus luteus L.) root nodules
was studied by electron paramagnetic resonance (EPR) spectroscopy. This pro
tein was capable of reducing oxidized leghemoglobin (Lb) in the presence of
NADH. The isolated nonheme iron protein, Lb reductase, was characterized b
y an EPR signal with g 1.94, which indicates the attribution of this protei
n to the Fe-S group of proteins.