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首页> 外文期刊>Journal of bacteriology >Biochemical Characterization of Individual Components of the Allochromatium vinosum DsrMKJOP Transmembrane Complex Aids Understanding of Complex Function In Vivo
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Biochemical Characterization of Individual Components of the Allochromatium vinosum DsrMKJOP Transmembrane Complex Aids Understanding of Complex Function In Vivo

机译：变色菌DsrMKJOP跨膜复合物单个成分的生化特征有助于体内复杂功能的理解

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The DsrMKJOP transmembrane complex has a most important function in dissimilatory sulfur metabolism and consists of cytoplasmic, periplasmic, and membrane integral proteins carrying FeS centers and b- and c-type cytochromes as cofactors. In this study, the complex was isolated from the purple sulfur bacterium Allochromatium vinosum and individual components were characterized as recombinant proteins. The two integral membrane proteins DsrM and DsrP were successfully produced in Escherichia coli C43(DE3) and C41(DE3), respectively. DsrM was identified as a diheme cytochrome b, and the two hemes were found to be in low-spin state. Their midpoint redox potentials were determined to be +60 and +110 mV. Although no hemes were predicted for DsrP, it was also clearly identified as a b-type cytochrome. To the best of our knowledge, this is the first time that heme binding has been experimentally proven for a member of the NrfD protein family. Both cytochromes were partly reduced after addition of a menaquinol analogue, suggesting interaction with quinones in vivo. DsrO and DsrK were both experimentally proven to be FeS-containing proteins. In addition, DsrK was shown to be membrane associated, and we propose a monotopic membrane anchoring for this protein. Coelution assays provide support for the proposed interaction of DsrK with the soluble cytoplasmic protein DsrC, which might be its substrate. A model for the function of DsrMKJOP in the purple sulfur bacterium A. vinosum is presented.
机译：DsrMKJOP跨膜复合物在异化硫代谢中具有最重要的功能，由携带FeS中心和 b -和 c 型细胞色素的细胞质，周质和膜整合蛋白组成。辅助因子。在这项研究中，该复合物是从紫色硫细菌 Allochromatium v​​inosum 中分离出来的，单个成分被表征为重组蛋白。两种整合膜蛋白DsrM和DsrP分别在大肠杆菌 C43（DE3）和C41（DE3）中成功产生。 DsrM被鉴定为双血红素细胞色素 b ，并且发现这两个血红素处于低旋态。他们的中点氧化还原电位被确定为+60和+110 mV。尽管没有预测DsrP的血红素，但也清楚地将其识别为 b 型细胞色素。据我们所知，这是首次针对NrfD蛋白家族成员进行血红素结合实验。添加甲萘醌类似物后，两种细胞色素均部分减少，表明与醌体内相互作用。 DsrO和DsrK均通过实验证明是含FeS的蛋白质。此外，DsrK被证明是与膜相关的，我们提出了该蛋白的单分子膜锚定。共洗脱分析为拟议的DsrK与可能是其底物的可溶性细胞质蛋白DsrC相互作用提供了支持。 DsrMKJOP在紫色硫细菌 A中的功能模型。介绍了葡萄籽。

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