Hirasawa M, Gray K A, Sung J D, Knaff D B
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock 79409-1061.
Arch Biochem Biophys. 1989 Nov 15;275(1):1-10. doi: 10.1016/0003-9861(89)90342-1.
The molecular weight of the spinach chloroplast, ferredoxin-dependent enzyme ferredoxin:nitrite oxidoreductase (EC 1.7.7.1) was shown to be 85,000 using gel filtration chromatography under nondenaturing conditions. In the presence of denaturants, either gel filtration chromatography or gel electrophoresis separated the enzyme into two subunits, with molecular weights of 61,000 and 24,000, respectively. Oxidation-reduction titrations of the siroheme prosthetic group of the putative native form (Mr 85,000) of the enzyme yielded a midpoint potential value of -305 mV, a value considerably more negative than the value of -30 mV obtained for siroheme in a modified, Mr 61,000 form of the enzyme.
在非变性条件下，使用凝胶过滤色谱法测得菠菜叶绿体中铁氧还蛋白依赖性酶铁氧还蛋白：亚硝酸氧化还原酶（EC 1.7.7.1）的分子量为85,000。在变性剂存在的情况下，无论是凝胶过滤色谱法还是凝胶电泳都将该酶分离成两个亚基，分子量分别为61,000和24,000。对该酶假定天然形式（Mr 85,000）的丝氨酸血红素辅基进行氧化还原滴定，得到的中点电位值为-305 mV，该值比在该酶的修饰形式（Mr 61,000）中丝氨酸血红素获得的-30 mV值要负得多。
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