Skip to main content
Log in

Differentiation of the multiple S- and N-oxide-reducing activities ofEscherichia coli

  • Published:
Current Microbiology Aims and scope Submit manuscript

Abstract

InEscherichia coli, several terminal reductases catalyze the reduction of S- and N-oxide compounds. We have used mutants missing either the constitutive dimethylsulfoxide (DMSO) reductase,dmsABC, and/or the inducible trimethylamine N-oxide (TMAO) reductase,torA, to define the roles of each reductase. These studies indicated that the constitutive DMSO reductase can sustain growth on DMSO, TMAO, methionine sulfoxide (MetSO), and other N-oxide compounds. Only one inducible TMAO reductase is expressed inE. coli, and this enzyme sustains growth on TMAO but not DMSO or MetSO. Characterization of atorA , dmsdouble mutant revealed that adenosine N-oxide (ANO) reductase is specifically required for anaerobic respiration on ANO in this mutant.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Literature Cited

  1. Bilous PT, Weiner JH (1985) Proton translocation coupled to dimethyl sulfoxide reduction in anaerobically grownEscherichia coli HB101. J Bacteriol 163:369–375

    Google Scholar 

  2. Bilous PT, Weiner JH (1988) Molecular cloning and expression of theEscherichia coli dimethyl sulfoxide reductase operon. J Bacteriol 170:1511–1518

    Google Scholar 

  3. Bilous PT, Cole ST, Anderson WF, Weiner JH (1988) Nucleotide sequence of thedmsABC operon encoding the anaerobic dimethyl sulfoxide reductase ofEscherichia coli. Mol Microbiol 2:785–795

    Google Scholar 

  4. Bragg D, Hackett NR (1983) Cytochromes of the trimethylamine N-oxide anaerobic respiratory pathway ofEscherichia coli. Biochim. Biophys. Acta 725:168–177

    Google Scholar 

  5. Condon C, Weiner JH (1988) Fumarate reductase ofEscherichia coli: an investigation of function and assembly using in vivo complementation. Mol Microbiol 2:43–52.

    Google Scholar 

  6. Ejin SI, Weissbach H, Brot N (1979) Reduction of methionione sulfoxide to methionine byEscherichia coli. J Bacteriol 139:161–164

    Google Scholar 

  7. Ferguson SJ, Page MD (1990) The functions and biosynthesis of thec-type cytochromes of bacterial respiratory chains with particular reference to autotrophs and the handling of C1 compounds. FEMS Microbiol Rev 87:227–234

    Google Scholar 

  8. Jasin M, Schimmel P (1984) Deletion of an essential gene inEscherichia coli by site-specific recombination with linear DNA fragments. J Bacteriol 159:783–786

    Google Scholar 

  9. Kelly DP, Baker SC (1990) The organosulfur cycle: aerobic and anaerobic processes leading to turnover of C1-sulfur compounds. FEMS Microbiol Rev 87:241–246

    Google Scholar 

  10. Kurihara FN, Satoh T (1988) A single enzyme is responsible for both dimethylsulfoxide and trimethylamine N-oxide respirations as the terminal reductase in a photodenitrifier,Rhodobacter sphaeroides f.s. denitrificans. Plant Cell Physiol 29:377–379

    Google Scholar 

  11. Markwell MA, Haas KSM, Bieber LL, Tolbert NE (1978) A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem 87:206–210

    Google Scholar 

  12. Miller JH (1972) Experiments in molecular genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory

    Google Scholar 

  13. Pascal MC, Bierne JF, Chippaux M (1984) Regulation of trimethylamine N-oxide (TMAO) reductase inEscherichia coli: Analysis oftor::Mud` operon fusion. Mol Gen Genet 195:351–355

    Google Scholar 

  14. Sagai M, Ishimoto M (1973) An enzyme reducing adenosine1N-oxide inEscherichia coli, amine N-oxide reductase. J Biochem 73:843–859

    Google Scholar 

  15. Sambasivarao D, Scraba DG, Trieber C, Weiner JH (1990) Organization of dimethylsulfoxide reductase in the plasma membrane ofEscherichia coli. J Bacteriol 172:5938–5948

    Google Scholar 

  16. Shimokawa O, Ishimoto M (1979) Purification and some properties of inducible tertiary amine N-oxide reductase fromEscherichia coli. J Biochem 86:1709–1717

    Google Scholar 

  17. Silvestro A, Pommier J, Giordano G (1988) The inducible trimethylamine N-oxide reductase ofEscherichia coli K12: biochemical and immunological studies. Biochim Biophys Acta 954:1–13

    Google Scholar 

  18. Silvestro A, Pommier J, Pascal MC, Giordano G (1989) The inducible trimethylamine N-oxide reductase ofEscherichia coli K12: its localization and inducers. Biochim Biophys Acta 999:208–216

    Google Scholar 

  19. Stewart V (1988) Nitrate respiration in relation to facultative metabolism in enterobacteria. Microbiol Rev 52:190–232

    Google Scholar 

  20. Takagi M, Ishimoto M (1983)Escherichia coli mutants defective in trimethylamine N-oxide reductase. FEMS Microbiol Lett 17:247–250

    Google Scholar 

  21. Takagi M, Tsuchiya T, Ishimoto M (1981) Proton translocation coupled to trimethylamine N-oxide reduction in anaerobically grownEscherichia coli. J Bacteriol 148:762–768

    Google Scholar 

  22. Weiner JH, MacIsaac DP, Bishop RE, Bilous PT (1988) Purification and properties ofEscherichia coli dimethylsulfoxide reductase, an iron-sulfur molybdoenzyme with broad substrate specificity. J Bacteriol 170:1505–1510

    Google Scholar 

  23. Yamamoto I, Okubo N, Ishimoto M (1986) Further characterization of trimethylamine N-oxide reductase fromEscherichia coli, a molybdoprotein. J Biochem 99:1773–1779

    Google Scholar 

  24. Yamamoto I, Hinakura M, Seki S, Seki Y, Kondo H (1989) Reduction of N-oxide and S-oxide compounds byEscherichia coli. J Gen Appl Microbiol 35:253–259

    Google Scholar 

  25. Yamamoto I, Hinakura M, Seki S, Seki Y, Kobndo H (1990) Anaerobic induction of trimethylamine N-oxide reductase and cytochromes by dimethylsulfoxide inEscherichia coli. Curr Microbiol 20:245–249

    Google Scholar 

  26. Yamamoto I, Yamazaki N, Hohmura M, Ishimoto M (1990) Effect oftor mutation inEscherichia coli on the trimethylamine N-oxide, nitrate and dimethyl sulfoxide reductases, the formate dehydrogenases N and H and nitrate repression. J Gen Appl Microbiol 36:357–363

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Sambasivarao, D., Weiner, J.H. Differentiation of the multiple S- and N-oxide-reducing activities ofEscherichia coli . Current Microbiology 23, 105–110 (1991). https://doi.org/10.1007/BF02092258

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02092258

Keywords

Navigation