Date of this Version
Plant Physiol. (1991) 96, 32-37
A ferric leghemoglobin reductase from the cytosol of soybean (Glyclne max) root nodules was purified to homogeneity and partlafly characterized. The enzyme is a flavoprotein with flavin adenine dinuclotide as the prosthetic group and consists of two identical subunits, each having a molecular mass of 54 kilodaltons. The pure enzyme shows a high activity for ferric leghemoglobin reduction with NADH as the reductant in the absence of any exogenous mediators. The enzyme also exhibits NADH-dependent 2,6-dichloroindophenol reductase activity. A sequence of the first 50 N-terminal amino acids of the purified protein was obtained. Comparisons with known protein sequences have shown that the sequence of the ferric leghemoglobin reductase is highly related to those of the flavin-nucleotide disulfide oxidoreductases, especially dihydrolipoamide dehydrogenase of the pyruvate dehydrogenase complex.