Hutson K G, Rogers L J, Haslett B G, Boulter D, Cammack R
Biochem J. 1978 Jun 15;172(3):465-77. doi: 10.1042/bj1720465.
Two ferredoxins were isolated from the cyanobacterium Nostoc strain MAC grown autotrophically in the light or heterotrophically in the dark. In either case approximately three times as much ferredoxin I as ferredoxin II was obtained. Both ferredoxins had absorption maxima at 276, 282 (shoulder), 330, 423 and 465 nm in the oxidized state, and each possessed a single 2 Fe-2S active centre. Their isoelectric points were approx. 3.2. The midpoint redox potentials of the ferredoxins differed markedly; that of ferredoxin I was --350mV and that of ferredoxin II was --445mV, at pH 8.0. The midpoint potential of ferredoxin II was unusual in being pH dependent. Ferredoxin I was most active in supporting NADP+ photoreduction by chloroplasts, whereas ferredoxin II was somewhat more active in pyruvate decarboxylation by the phosphoroclastic system of Clostridum pasteurianum. Though the molecular weights of the ferredoxins determined by ultracentrifugation were the same within experimetnal error, the amino acid compositions showed marked differences. The N-terminal amino acid sequences of ferredoxins I and II were determined by means of an automatic sequencer. There are 11--12 differences between the sequences of the first 32 residues. It appears that the two ferredoxins have evolved separately to fulfil different roles in the organism.
从在光照下自养生长或在黑暗中异养生长的蓝细菌念珠藻菌株MAC中分离出了两种铁氧化还原蛋白。在这两种情况下,获得的铁氧化还原蛋白I的量大约是铁氧化还原蛋白II的三倍。两种铁氧化还原蛋白在氧化态时的吸收峰分别位于276、282(肩峰)、330、423和465nm处,并且每种都具有一个单一的2Fe-2S活性中心。它们的等电点约为3.2。两种铁氧化还原蛋白的中点氧化还原电位有显著差异;在pH 8.0时,铁氧化还原蛋白I的中点氧化还原电位为-350mV,铁氧化还原蛋白II的为-445mV。铁氧化还原蛋白II的中点电位不同寻常,它依赖于pH值。铁氧化还原蛋白I在支持叶绿体进行NADP+光还原方面最具活性,而铁氧化还原蛋白II在巴氏梭菌的磷酸裂解系统进行丙酮酸脱羧反应中活性稍高。尽管通过超速离心法测定的两种铁氧化还原蛋白的分子量在实验误差范围内相同,但氨基酸组成显示出显著差异。通过自动测序仪测定了铁氧化还原蛋白I和II的N端氨基酸序列。在前32个残基的序列之间有11 - 12个差异。看来这两种铁氧化还原蛋白是分别进化的,以便在生物体中发挥不同的作用。