来自热醋酸梭菌的具有高热稳定性的四铁四硫铁氧还蛋白。
A four-iron, four-sulfide ferredoxin with high thermostability from Clostridium thermoaceticum.
作者信息
Yang S S, Ljungdahl L G, LeGall J
出版信息
J Bacteriol. 1977 Jun;130(3):1084-90. doi: 10.1128/jb.130.3.1084-1090.1977.
Abstract
A ferredoxin containing only one [Fe4S4] cluster was purified from Clostridium thermoaceticum. It has a molecular weight of about 7,300, a partial specific volume of 0.67, and an isoelectric point of 3.25. Its absorption spectrum has two maxima at 390 nm (epsilon = 16.8 X 10(3)M-1cm-1) and at 280 nm (epsilon = 24.2 X 10(3)M-1cm-1). The absorption at 390 nm is almost half that of other clostridial ferredoxins, which have two [Fe4S4] clusters, and is similar to other ferredoxins with only one [Fe4S4] cluster. The ferredoxin had high thermal stability and retained over 50% of its activity after treatment at 80 degrees C. It functions in the transfer of electrons from pyruvate to nicotinamide adenine dinucleotide phosphate (NADP), which indicates the presence of pyruvate:ferredoxin oxidoreductase and reduced ferredoxin-NADP reductase in C, thermoaceticum. NADPH is used in the synthesis of acetate from CO2 in this organism.
摘要
从热醋梭菌中纯化出一种仅含有一个[Fe4S4]簇的铁氧化还原蛋白。它的分子量约为7300，比容为0.67，等电点为3.25。其吸收光谱在390nm（ε = 16.8×10³M⁻¹cm⁻¹）和280nm（ε = 24.2×10³M⁻¹cm⁻¹）处有两个最大值。390nm处的吸收几乎是其他含有两个[Fe4S4]簇的梭菌铁氧化还原蛋白的一半，与其他仅含有一个[Fe4S4]簇的铁氧化还原蛋白相似。该铁氧化还原蛋白具有很高的热稳定性，在80℃处理后仍保留超过50%的活性。它在电子从丙酮酸转移到烟酰胺腺嘌呤二核苷酸磷酸（NADP）的过程中起作用，这表明热醋梭菌中存在丙酮酸：铁氧化还原蛋白氧化还原酶和还原型铁氧化还原蛋白-NADP还原酶。NADPH用于该生物体中由CO₂合成乙酸盐的过程。
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