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. 1991 May;96(1):32–37. doi: 10.1104/pp.96.1.32

Purification and Characterization of Soybean Root Nodule Ferric Leghemoglobin Reductase 1

Lin Ji 1, Stephen Wood 1, Manuel Becana 1,2, Robert V Klucas 1
PMCID: PMC1080709  PMID: 16668174

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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