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首页> 外文期刊>Journal of bacteriology >Characterization of a cytochrome a1 that functions as a ubiquinol oxidase in Acetobacter aceti.
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Characterization of a cytochrome a1 that functions as a ubiquinol oxidase in Acetobacter aceti.

机译：细胞色素a1的特征，该色素在醋杆菌中起泛醇氧化酶的作用。

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The terminal oxidase for ethanol oxidation in Acetobacter aceti was purified as a complex consisting of four subunits (subunits I, II, III, and IV) with molecular masses of 72, 34, 21, and 13 kDa, respectively. Spectrophotometric analysis and catalytic properties determined with the purified enzyme showed that it belonged to a family of cytochrome a1 (ba)-type ubiquinol oxidases. A polymerase chain reaction with two oligonucleotides designed for amino acid sequences that are conserved in subunit I of the aa3-type cytochrome c oxidases from various origins and of an Escherichia coli o (bo)-type ubiquinol oxidase was used for cloning the cytochrome a1 gene. A 0.5-kb fragment thus amplified was used as the probe to clone a 4.5-kb KpnI fragment that contained a putative open reading frame for the whole subunit I gene. The molecular weight and amino acid composition of the product of this open reading frame (cyaA) were the same as those of the purified protein from A. aceti. The amino acid sequence of CyaA was homologous to that of subunit I of the E. coli o-type ubiquinol oxidase. Nucleotide sequence analysis of the region neighboring the cyaA gene revealed that the genes (cyaB, cyaC, and cyaD) encoding the other three subunits (subunits II, III, and IV) were clustered upstream and downstream of the cyaA gene in the order cyaB, cyaA, cyaC, and cyaD and with the same transcription polarity, forming an operon. As expected from the enzymatic properties, CyaB, CyaC, and CyaD showed great similarity in amino acid sequence to the corresponding sununits of the E. coli o-type ubiquinol oxidase and as(3)-type cytochrome c oxidases.
机译：纯化醋醋杆菌中用于乙醇氧化的末端氧化酶，以复合物的形式纯化，该复合物由分子量分别为72、34、21和13 kDa的四个亚基（亚基I，II，III和IV）组成。纯化的酶的分光光度分析和催化性能表明，它属于细胞色素a1（ba）型泛醇氧化酶家族。使用两个设计用于氨基酸序列的寡核苷酸的聚合酶链式反应，该氨基酸序列保存在来自不同来源的aa3型细胞色素c氧化酶亚基和大肠杆菌o（bo）型泛醌氧化酶的亚基I中，用于克隆细胞色素a1基因。将如此扩增的0.5kb片段用作探针，以克隆4.5kb KpnI片段，该片段含有假定的整个亚基I基因的开放阅读框。该开放阅读框（cyaA）产物的分子量和氨基酸组成与从醋曲霉中纯化的蛋白质的分子量和氨基酸组成相同。 CyaA的氨基酸序列与大肠杆菌o型泛醌氧化酶的亚基I同源。对cyaA基因附近区域的核苷酸序列分析表明，编码其他三个亚基（亚基II，III和IV）的基因（cyaB，cyaC和cyaD）以cyaB顺序聚集在cyaA基因的上游和下游， cyaA，cyaC和cyaD并具有相同的转录极性，形成操纵子。正如从酶学性质所预期的那样，CyaB，CyaC和CyaD在氨基酸序列上与大肠杆菌o型泛醌氧化酶和as（3）型细胞色素c氧化酶的相应太阳单位表现出极大的相似性。

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