Hase T, Matsubara H, Hutber G N, Rogers L J
J Biochem. 1982 Nov;92(5):1347-55. doi: 10.1093/oxfordjournals.jbchem.a134058.
The amino acid sequences of ferredoxins I and II from a blue-green alga, Nostoc strain MAC were determined. This alga is able to grow autotrophically in the light or heterotrophically in the dark. Analyses of tryptic peptides of Cm-proteins by conventional methods including solid-phase Edman degradation gave the complete amino acid sequences. Both molecules consisted of 98 amino acid residues and 34 amino acid differences including two deletions were found between the two. Comparing these sequences with those of ferredoxins from Chlorogloeopsis fritschii and Synechocystis 6714, which are also capable of growing under both conditions, showed that Nostoc strain MAC ferredoxin II had unique amino acids around the [2Fe-2S] cluster. This finding provides a structural basis for explaining the different chemical and functional properties of Nostoc strain MAC ferredoxin II reported in a previous paper (Hutson et al. (1978) Biochem. J. 172, 465-477).
测定了蓝藻念珠藻菌株MAC的铁氧化还原蛋白I和II的氨基酸序列。这种藻类能够在光照下自养生长,或在黑暗中异养生长。通过包括固相埃德曼降解在内的常规方法对Cm-蛋白的胰蛋白酶肽段进行分析,得出了完整的氨基酸序列。两种分子均由98个氨基酸残基组成,两者之间发现了34个氨基酸差异,包括两个缺失。将这些序列与同样能够在两种条件下生长的弗里奇绿胶藻和聚球藻6714的铁氧化还原蛋白序列进行比较,结果表明,念珠藻菌株MAC铁氧化还原蛋白II在[2Fe-2S]簇周围具有独特的氨基酸。这一发现为解释先前论文(Hutson等人,(1978年)《生物化学杂志》172卷,465 - 477页)中报道的念珠藻菌株MAC铁氧化还原蛋白II的不同化学和功能特性提供了结构基础。