LeGall J, Liu M Y, Gomes C M, Braga V, Pacheco I, Regalla M, Xavier A V, Teixeira M
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
FEBS Lett. 1998 Jun 16;429(3):295-8. doi: 10.1016/s0014-5793(98)00610-3.
A new rubredoxin from the sulphate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774, grown with nitrate as terminal electron acceptor, was isolated and characterised. The protein is an 8.5 kDa monomer containing one iron atom per molecule, with a reduction potential of 25 +/- 5 mV at pH 7.6. Like the recombinant Rdl protein from D. vulgaris, expressed in Escherichia coli [Lumpio, H.L., Shenvi, N.V., Garg, R.P., Summers, A.O. and Kurtz, D.M., J. Bacteriol. 179 (1997) 4607-4615], it contains an unusual spacing of four amino acids between the first two of the iron coordinating cysteinyl residues. This difference is reflected in the structure of the iron centre, as observed by visible and EPR spectroscopies. All together, these features make these proteins the first members of a new family of rubredoxins.
从以硝酸盐作为末端电子受体生长的脱硫弧菌脱硫脱硫弧菌ATCC 27774中分离并鉴定了一种新的红氧还蛋白。该蛋白质是一种8.5 kDa的单体，每个分子含有一个铁原子，在pH 7.6时还原电位为25±5 mV。与在大肠杆菌中表达的来自普通脱硫弧菌的重组Rdl蛋白[Lumpio, H.L., Shenvi, N.V., Garg, R.P., Summers, A.O.和Kurtz, D.M., 《细菌学杂志》179 (1997) 4607 - 4615]一样，它在第一个和第二个铁配位半胱氨酸残基之间含有四个氨基酸的不寻常间隔。如通过可见光谱和电子顺磁共振光谱所观察到的，这种差异反映在铁中心的结构中。总之，这些特征使这些蛋白质成为新的红氧还蛋白家族的首批成员。
