聚球藻6301（集胞藻）可溶性铁氧化还原蛋白的性质和结构。与基因序列的关系。
Properties and structure of the soluble ferredoxin from Synechococcus 6301 (Anacystis nidulans). Relationship to gene sequences.
作者信息
Wada K, Masui R, Matsubara H, Rogers L J
机构信息
Department of Biology, Osaka University, Japan.
出版信息
Biochem J. 1988 Jun 1;252(2):571-5. doi: 10.1042/bj2520571.
Photoautotrophic cultures of the unicellular cyanobacterium Synechococcus 6301 (Anacystis nidulans) possessed a single [2Fe-2S] ferredoxin with a midpoint redox potential of -385 mV. Determination of the amino acid sequence of the ferredoxin showed that it consisted of 98 residues, with methionine and tryptophan both absent, and with only the four cysteine residues that are required to co-ordinate the iron-sulphur cluster. Comparisons with other ferredoxin sequences showed that most resemblance was to those from filamentous cyanobacteria, with up to 87% homology. There was less resemblance to the ferredoxins of unicellular cyanobacteria, with 25 differences when compared with that from another Synechococcus sp. However, the sequence of Synechococcus 6301 ferredoxin was identical with that derived for a gene sequence for a putative ferredoxin from the genotypically closely related Synechococcus 7942 (Anacystis nidulans R2). In contrast, the sequence showed substantial differences from that corresponding to a putative ferredoxin gene from Synechococcus 6301 reported by Cozens & Walker [(1988) Biochem. J. 252, 563-569].
单细胞蓝细菌聚球藻6301（集胞藻）的光合自养培养物含有一种单一的[2Fe-2S]铁氧化还原蛋白，其氧化还原中点电位为-385 mV。对该铁氧化还原蛋白的氨基酸序列测定表明，它由98个残基组成，既没有甲硫氨酸也没有色氨酸，且只有配位铁硫簇所需的四个半胱氨酸残基。与其他铁氧化还原蛋白序列的比较表明，它与丝状蓝细菌的序列最为相似，同源性高达87%。与单细胞蓝细菌的铁氧化还原蛋白的相似性较低，与另一种聚球藻属物种的铁氧化还原蛋白相比有25个差异。然而，聚球藻6301铁氧化还原蛋白的序列与从基因型密切相关的聚球藻7942（集胞藻R2）的一个假定铁氧化还原蛋白的基因序列推导出来的序列相同。相比之下，该序列与Cozens和Walker [（1988年）《生物化学杂志》252, 563 - 569]报道的聚球藻6301的一个假定铁氧化还原蛋白基因的相应序列有很大差异。
Zotero 插件