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A non-haem iron protein was isolated from an extract of soya-bean nodule bacteroids by a procedure including protamine sulphate and heat precipitation followed by chromatography on DEAE-cellulose. The purified protein contains non-haem iron and acid-labile sulphur and exhibits a spectrum with a rather broad absorption shoulder in the region 380-440nm and a more prominent peak at 280nm. From sedimentation-velocity measurements an apparent s(20,w) value of 1.3S was calculated. The protein functions as an electron carrier between the reducing system of illuminated chloroplast fragments and nitrogenase from nodule bacteroids, but it failed to function as a cofactor for the photochemical reduction of NADP in the presence of spinach chloroplasts. Also, it is inactive as a cofactor in the enzymic degradation of pyruvate to acetyl phosphate and CO(2) in the presence of a ferredoxin-free extract of Clostridium pasteurianum. Repeated freezing, storage and thawing of the non-haem iron protein resulted in a marked loss of activity in the photochemical acetylene-reduction assay. A major portion of the activity that was lost was restored as a result of treatment with sodium sulphide, mercaptoethanol and ferrous ammonium sulphate.

Purification and some properties of a non-haem iron protein from the bacteroids of soya-bean (Glycine max Merr.) nodules