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Plant Physiology 96:32-37 (1991)
© 1991 American Society of Plant Biologists

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Metabolism and Enzymology

Purification and Characterization of Soybean Root Nodule Ferric Leghemoglobin Reductase 1

Lin Ji, Stephen Wood, Manuel Becana2 and Robert V. Klucas

Department of Biochemistry and School of Biological Science, University of Nebraska-Lincoln, Lincoln, Nebraska 68583-0718

A ferric leghemoglobin reductase from the cytosol of soybean (Glycine max) root nodules was purified to homogeneity and partially characterized. The enzyme is a flavoprotein with flavin adenine dinucleotide 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 oxido-reductases, especially dihydrolipoamide dehydrogenase of the pyruvate dehydrogenase complex.

2 Permanent address: Laboratorio de Fijación de Nitrógeno, E.E. Aula Dei, Apdo. 202, 50080 Zaragoza, Spain.

1 Journal Series No. 9404, Agricultural Research Division, University of Nebraska.




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J. F. Moran, Z. Sun, G. Sarath, R. Arredondo-Peter, E. K. James, M. Becana, and R. V. Klucas
Molecular Cloning, Functional Characterization, and Subcellular Localization of Soybean Nodule Dihydrolipoamide Reductase
Plant Physiology, January 1, 2002; 128(1): 300 - 313.
[Abstract] [Full Text] [PDF]


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Copyright © 1991 by the American Society of Plant Biologists