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首页> 外文期刊>Biochemistry >DsrJ, an Essential Part of the DsrMKJOP Transmembrane Complex in the Purple Sulfur Bacterium Allochromatium vinosum, Is an Unusual Triheme Cytochrome c
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DsrJ, an Essential Part of the DsrMKJOP Transmembrane Complex in the Purple Sulfur Bacterium Allochromatium vinosum, Is an Unusual Triheme Cytochrome c

机译：DsrJ是紫色硫细菌异色变色菌中DsrMKJOP跨膜复合物的重要组成部分，是一种异常的Triheme细胞色素c

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TheDsrMKJOP transmembrane complex has amost important function in dissimilatory sulfurnmetabolism, not only in many sulfur-oxidizing organisms but also in sulfate-reducing prokaryotes. Here,nwe focused on an individual component of this complex, the triheme cytochrome c DsrJ from the purplensulfur bacterium Allochromatium vinosum.In A. vinosum, the signal peptide of DsrJ is not cleaved off butnserves as a membrane anchor. Sequence analysis suggested the presence of three heme c species with bis-nHis, His/Met, and possibly a very unusual His/Cys ligation. A. vinosum DsrJ produced as a recombinantnprotein in Escherichia coli indeed contained three hemes, and electron paramagnetic resonance (EPR)nspectroscopy provided evidence of possible, but only partial, His/Cys heme ligation in one of the hemes.nThis heme shows heterogeneous coordination, withMet being another candidate ligand. Cysteine 46 wasnreplaced with serine using site-directed mutagenesis, with the mutant protein showing a small decrease innthe magnitude of the EPR signal attributed to His/Cys coordination, but identical UV-vis and RR spectra.nThe redox potentials of the hemes in the wild-type protein were determined to be -20, -200, and -220 mVnand were found to be virtually identical in the mutant protein. However, in vivo the same ligand exchangenled to a dramatically altered phenotype, highlighting the importance of Cys46. Our results suggest thatnCys46 may be involved in catalytic sulfur chemistry rather than electron transfer. Additional in vivonexperiments showed that DsrJ can be functionally replaced in A. vinosum by the homologous protein fromnthe sulfate reducer Desulfovibrio vulgaris
机译：DsrMKJOP跨膜复合物不仅在多种硫氧化生物中而且在还原硫酸盐的原核生物中都在异化硫代谢中具有最重要的功能。在此，我们集中研究了这种复合物的单个成分，即紫色硫细菌异色菌的三血红素细胞色素c DsrJ。在A. vinosum中，DsrJ的信号肽没有被切开，而是充当了膜锚。序列分析表明存在三个带有双-nHis，His / Met的血红素物种，可能是非常不寻常的His / Cys连接。在大肠杆菌中作为重组蛋白生产的A. vinosum DsrJ确实包含三个血红素，电子顺磁共振（EPR）n光谱学提供了在其中一个血红素中可能（但仅部分）His / Cys血红素连接的证据.n该血红素显示异质配位， Met是另一个候选配体。使用定点诱变法将半胱氨酸46替换为丝氨酸，突变蛋白显示归因于His / Cys配位的EPR信号强度的小幅下降，但具有相同的UV-vis和RR光谱.n野生血红素的氧化还原电位突变型蛋白中的-型蛋白被确定为-20，-200和-220mV·n，并且实际上是相同的。然而，在体内相同的配体交换为显着改变的表型，突出了Cys46的重要性。我们的结果表明，nCys46可能参与催化硫化学反应，而不是电子转移。其他体内实验表明，DsrJ可以在功能性置换中被来自硫酸盐还原剂Desulfovibrio vulgaris的同源蛋白取代。

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    《Biochemistry》 |2010年第38期|p.8290-8299|共10页
  • 作者

    Fabian Grein Sofia S. Venceslau Lilian Schneider Peter Hildebrandt Smilja Todorovic Ins A. C. Pereira and Christiane Dahl;

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    ‡Institut f€ ur Mikrobiologie & Biotechnologie, Rheinische Friedrich-Wilhelms-Universit€ at Bonn, Meckenheimer Allee 168,D-53115 Bonn, Germany,§Instituto de Tecnologia Quı ´mica e Biolu0002 ogica, Universidade Nova de Lisboa, Avenida da Republica, EAN,Apt 127, 2780-157 Oeiras, Portugal, and ) Technische Universit€ at Berlin, Institut f€ ur Chemie, Sekr. PC14,Strasse des 17. Juni 135, 10623 Berlin, Germany;

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