Devreese B, Costa C, Demol H, Papaefthymiou V, Moura I, Moura J J, Van Beeumen J
Department of Biochemistry, Physiology and Microbiology, University of Gent, Belgium.
Eur J Biochem. 1997 Sep 1;248(2):445-51. doi: 10.1111/j.1432-1033.1997.00445.x.
The complete amino acid sequence of the unusual diheme split-Soret cytochrome c from the sulphate-reducing Desulfovibrio desulfuricans strain ATCC 27774 has been determined using classical chemical sequencing techniques and mass spectrometry. The 247-residue sequence shows almost no similarity with any other known diheme cytochrome c, but the heme-binding site of the protein is similar to that of the cytochromes c3 from the sulphate reducers. The cytochrome-c-like domain of the protein covers only the C-terminal part of the molecule, and there is evidence for at least one more domain containing four cysteine residues, which might bind another cofactor, possibly a non-heme iron-containing cluster. This domain is similar to a sequence fragment of the genome of Archaeoglobus fulgidus, which confirms the high conservation of the genes involved in sulfate reduction.
利用经典化学测序技术和质谱分析法，已确定了来自硫酸盐还原菌脱硫脱硫弧菌（Desulfovibrio desulfuricans）菌株ATCC 27774的异常双血红素裂分-索雷特细胞色素c的完整氨基酸序列。该247个残基的序列与任何其他已知的双血红素细胞色素c几乎没有相似性，但该蛋白质的血红素结合位点与硫酸盐还原菌的细胞色素c3的血红素结合位点相似。该蛋白质的细胞色素c样结构域仅覆盖分子的C末端部分，并且有证据表明至少还有一个包含四个半胱氨酸残基的结构域，该结构域可能结合另一种辅因子，可能是一个含非血红素铁的簇。该结构域与嗜热栖热菌（Archaeoglobus fulgidus）基因组的一个序列片段相似，这证实了参与硫酸盐还原的基因具有高度保守性。
