Studies of the ferredoxin from Thermus thermophilus.

Abstract

The soluble ferredoxin from Thermus thermophilus was examined by Mossbauer and EPR spectroscopies and by reductive titrations.These studies demonstrate the presence of one 3Fe center, responsible for the characteristic g = 2.02 EPR signal in the oxidized protein, and one [4Fe-4S] center which is responsible for the rhombic EPR spectrum of the fully reduced protein.These assignments should replace those made by Ohnishi et al. (