Archives of Microbiology

, Volume 173, Issue 3, pp 178–186

Involvement of the respiratory chain of gram-negative bacteria in the reduction of tellurite

  • Stella M. Trutko
  • Vasilii K. Akimenko
  • Nataliya E. Suzina
  • Lyudmila A. Anisimova
  • Mikhail G. Shlyapnikov
  • Boris P. Baskunov
  • Vitalii I. Duda
  • Aleksandr M. Boronin
Original Paper

DOI: 10.1007/s002039900123

Cite this article as:
Trutko, S., Akimenko, V., Suzina, N. et al. Arch Microbiol (2000) 173: 178. doi:10.1007/s002039900123

Abstract.

The terminal oxidases of the respiratory chain of seven strains of gram-negative bacteria were shown to be involved in the reduction of tellurite. The rate of tellurite reduction correlated with the intensity of respiration. The inhibitors of terminal oxidases, carbon monoxide and cyanide, inhibited the reduction of tellurite. In Pseudomonas aeruginosa PAO ML4262 and P. aeruginosa PAO ML4262 (pBS10), the respiratory chain was found to contain three types of cytochrome c, one of which (the carbon monoxide-binding cytochrome c) was involved in the reduction of tellurite. Agrobacterium tumefaciens VKM B-1219, P. aeruginosa IBPM B-13, and Escherichia coli G0-102bd++ cells contained oxidases aa3, bb3, and bd, respectively. The respiratory chain of other strains contained two oxidases: E. coli DH5α of bb3- and bd-type, and Erwinia carotovora VKM B-567 of bo3- and bd-type. All the strains under study reduced tellurite with the formation of tellurium crystallites. Depending on the position of the active center of terminal oxidases in the plasma membrane, the crystallites appeared either in the periplasmic space [P. aeruginosa PAO ML4262 and P. aeruginosa PAO ML4262 (pBS10)], or on the outer surface of the membrane (A. tumefaciens VKM B-1219 and P. aeruginosa IBPM B-13), its inner surface (E. coli G0-102bd++), or on both surfaces (E. coli DH5α and E. carotovora VKM B-567).

Bacteria Tellurite reduction Compartmentalization Tellurium crystallites R plasmids Respiratory chain Inhibitors Terminal oxidases Spectrophotometry Heme 

Copyright information

© Springer-Verlag 0000

Authors and Affiliations

  • Stella M. Trutko
    • 1
  • Vasilii K. Akimenko
    • 1
  • Nataliya E. Suzina
    • 1
  • Lyudmila A. Anisimova
    • 1
  • Mikhail G. Shlyapnikov
    • 1
  • Boris P. Baskunov
    • 1
  • Vitalii I. Duda
    • 1
  • Aleksandr M. Boronin
    • 1
  1. 1.Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, pr. Nauki 5, Pushchino, Moscow 142292, Russia

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