Guerlesquin F, Bruschi M, Bovier-Lapierre G, Fauque G
Biochim Biophys Acta. 1980 Nov 20;626(1):127-35. doi: 10.1016/0005-2795(80)90204-4.
Two ferredoxins isolated from Desulfovibrio desulfuricans Norway have been purified and characterized. The less acidic, designated as ferredoxin I, contains four iron atoms, four acid-labile sulfur groups and six cysteine residues per molecule. Ferredoxin II is more acidic and abundant than ferredoxin I, but is very unstable to O2. Ferredoxin I and ferredoxin II differ according to amino acid composition but are homologous with respect to their N-terminal amino acid sequence. The absorption spectra of the two ferredoxins are similar to those of other Desulfovibrio species. Both proteins appear to be dimers of identical 6000-dalton subunits. Their activity was tested in two types of reaction in the electron transfer chain (phosphoroclastic reaction and sulfite reductase activity). The isolation of two different ferredoxins from the same organism, Desulfovibrio, has been reported in Desulfovibrio africanus but the significance of two ferredoxins functioning in the same electron transfer chain is not yet understood.
从脱硫弧菌挪威菌株中分离出的两种铁氧化还原蛋白已得到纯化和表征。酸性较弱的一种被指定为铁氧化还原蛋白I,每个分子含有四个铁原子、四个酸不稳定硫基团和六个半胱氨酸残基。铁氧化还原蛋白II比铁氧化还原蛋白I酸性更强且含量更丰富,但对O2非常不稳定。铁氧化还原蛋白I和铁氧化还原蛋白II在氨基酸组成上有所不同,但在N端氨基酸序列方面具有同源性。这两种铁氧化还原蛋白的吸收光谱与其他脱硫弧菌属物种的光谱相似。这两种蛋白质似乎都是由相同的6000道尔顿亚基组成的二聚体。它们的活性在电子传递链中的两种反应(磷酸裂解反应和亚硫酸盐还原酶活性)中进行了测试。在非洲脱硫弧菌中也曾报道过从同一生物体脱硫弧菌中分离出两种不同的铁氧化还原蛋白,但尚未了解两种铁氧化还原蛋白在同一电子传递链中发挥作用的意义。