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NADH: 醌氧化还原酶亚基 NuoA 的跨膜取向的修订。

Revised transmembrane orientation of the NADH:quinone oxidoreductase subunit NuoA.

机构信息

Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, Lund, Sweden.

出版信息

FEBS Lett. 2011 Oct 20;585(20):3277-83. doi: 10.1016/j.febslet.2011.09.006. Epub 2011 Sep 14.

Abstract

NuoA is a small membrane spanning subunit of respiratory chain NADH:quinone oxidoreductase (complex I). Unlike the other complex I core protein subunits, the NuoA protein has no known homologue in other enzyme systems. The transmembrane orientation of NuoA cannot be unambiguously predicted, due to the small size of the polypeptide and the varying distribution of charged amino acid residues in NuoA from different organisms. Novel analyses of NuoA from Escherichia coli complex I expressed as fusion proteins to cytochrome c and to alkaline phosphatase demonstrated that the c-terminal end of the polypeptide is localized in the bacterial cytoplasm, in contrast to what was previously reported for the homologous NQO7 subunit from Paracoccus denitrificans complex I.

摘要

NuoA 是呼吸链 NADH:醌氧化还原酶(复合物 I)的一个小跨膜亚基。与其他复合物 I 核心蛋白亚基不同,NuoA 蛋白在其他酶系统中没有已知的同源物。由于多肽的小尺寸和不同生物体中 NuoA 带电荷氨基酸残基的分布变化,NuoA 的跨膜取向不能明确预测。对大肠杆菌复合物 I 中表达的 NuoA 融合蛋白与细胞色素 c 和碱性磷酸酶的新分析表明,该多肽的 C 末端位于细菌细胞质中,与先前报道的 Paracoccus denitrificans 复合物 I 中同源的 NQO7 亚基相反。

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