Ji L, Wood S, Becana M, Klucas R V
Department of Biochemistry and School of Biological Science, University of Nebraska-Lincoln, Lincoln, Nebraska 68583-0718.
Plant Physiol. 1991 May;96(1):32-7. doi: 10.1104/pp.96.1.32.
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.
从大豆（Glycine max）根瘤细胞质中纯化得到一种铁血红蛋白还原酶，并对其进行了部分特性鉴定。该酶是一种以黄素腺嘌呤二核苷酸为辅基的黄素蛋白，由两个相同的亚基组成，每个亚基的分子量为54千道尔顿。在没有任何外源介质的情况下，纯酶以NADH作为还原剂，对高铁血红蛋白还原表现出高活性。该酶还表现出依赖NADH的2,6-二氯靛酚还原酶活性。获得了纯化蛋白前50个N端氨基酸的序列。与已知蛋白质序列的比较表明，铁血红蛋白还原酶的序列与黄素核苷酸二硫化物氧化还原酶的序列高度相关，尤其是丙酮酸脱氢酶复合体的二氢硫辛酰胺脱氢酶。
