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Volume 152, Issue 2

SoxV transfers electrons to the periplasm of – an essential reaction for chemotrophic sulfur oxidation Free

Abstract

The genes are located upstream of the gene cluster encoding the sulfur-oxidizing ability of . SoxV is highly homologous to CcdA, which is involved in cytochrome maturation of . SoxV was shown to function in reduction of the periplasmic SoxW, which shows a CysXaaXaaCys motif characteristic for thioredoxins. From strain GBΩV, which carries an Ω-kanamycin-resistance-encoding interposon in , and complementation analysis it was evident that SoxV but not the periplasmic SoxW was essential for lithoautotrophic growth of with thiosulfate. However, the thiosulfate-oxidizing activities of cell extracts from the wild-type and from strain GBΩV were similar, demonstrating that the low thiosulfate-oxidizing activity of strain GBΩV was not due to a defect in biosynthesis or maturation of proteins of the Sox system and suggesting that SoxV is part of a regulatory or catalytic system of the Sox system. Analysis of DNA sequences available from different organisms harbouring a Sox system revealed that genes are exclusively present in operons harbouring the genes, encoding sulfur dehydrogenase, suggesting that SoxCD might be a redox partner of SoxV. No complementation of the mutant TP43 defective in cytochrome maturation was achieved by expression of , demonstrating that the high identity of SoxV and CcdA does not correspond to functional homology.

  • Received:
  • Accepted:
  • Revised:
  • Published Online:
Keyword(s): AMS, 4-acetamido-4′-maleimidylstilbene-2,2′-disulfonic acid , Sox, sulfur oxidation , TCEP, tris(2-carboxyethyl)phosphine and TMPD, N,N,N′,N′-tetramethyl-1,4-benzenediamine
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2006-02-01
2023-09-29
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SoxV transfers electrons to the periplasm of Paracoccus pantotrophus – an essential reaction for chemotrophic sulfur oxidation
Microbiology 152, 465 (2006); https://doi.org/10.1099/mic.0.28523-0
/content/journal/micro/10.1099/mic.0.28523-0
/content/journal/micro/10.1099/mic.0.28523-0
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