Pettigrew G W
Biochem J. 1974 May;139(2):449-59. doi: 10.1042/bj1390449.
Cytochrome c-552 from Euglena gracilis was purified and the amino acid sequence determined. The protein is a single peptide chain of 87 residues with the haem prosthetic group bound through two thioether linkages to two cysteine residues near the amino-terminal region. The amino acid sequence shows some similarities to mitochondrial cytochrome c and to two prokaryote c-type cytochromes. The sequence, taken with the known characteristics of cytochrome c-552, indicates that it is an f-type cytochrome. The possible functional and evolutionary significance of these features in common is discussed. Detailed evidence for the amino acid sequence of Euglena cytochrome f has been deposited as Supplementary Publication SUP 50027 at the British Library, Lending Division (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7QB, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973) 131, 5.
从纤细裸藻中纯化出细胞色素c-552,并测定了其氨基酸序列。该蛋白质是一条由87个残基组成的单肽链,血红素辅基通过两个硫醚键与氨基末端区域附近的两个半胱氨酸残基相连。氨基酸序列与线粒体细胞色素c以及两种原核生物c型细胞色素有一些相似之处。结合细胞色素c-552的已知特性来看,该序列表明它是一种f型细胞色素。文中讨论了这些共同特征可能具有的功能和进化意义。纤细裸藻细胞色素f氨基酸序列的详细证据已作为补充出版物SUP 50027存放在英国利兹市波士顿温泉市约克郡LS23 7QB的大英图书馆出借部(原国家科技出借图书馆),可按《生物化学杂志》(1973年)第131卷第5期所示条件从该处获取复印件。