This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Azarkina, N.
Right arrow Articles by Konstantinov, A. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Azarkina, N.
Right arrow Articles by Konstantinov, A. A.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 2002, p. 5339-5347, Vol. 184, No. 19
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.19.5339-5347.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Stimulation of Menaquinone-Dependent Electron Transfer in the Respiratory Chain of Bacillus subtilis by Membrane Energization

N. Azarkina and A. A. Konstantinov*

A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, Russia

Received 28 March 2002/ Accepted 27 June 2002

At a pH of <=7, respiration of Bacillus subtilis cells on endogenous substrates shut down almost completely upon addition of an uncoupler (carbonyl cyanide m-chlorophenylhydrazone [CCCP]) and a K+-ionophore (valinomycin). The same effect was observed with cell spheroplasts lacking the cell wall. The concentration of CCCP required for 50% inhibition of the endogenous respiration in the presence of K+-valinomycin was below 100 nM. Either CCCP or valinomycin alone was much less efficient than the combination of the two. The inhibitory effect was easily reversible and depended specifically on the H+ and K+ concentrations in the medium. Similar inhibition was observed with respect to the reduction of the artificial electron acceptors 2,6-dichlorophenolindophenol (DCPIP) and N,N,N',N'-tetramethyl-p-phenylenediamine cation (TMPD+), which intercept reducing equivalents at the level of menaquinol. Oxidation of the reduced DCPIP or TMPD in the bacterial cells was not sensitive to uncoupling. The same loss of the electron transfer activities as induced by the uncoupling was observed upon disruption of the cells during isolation of the membranes; the residual activities were not further inhibited by the uncoupler and ionophores. We conclude that the menaquinone-dependent electron transfer in the B. subtilis respiratory chain is facilitated, thermodynamically or kinetically, by membrane energization. A requirement for an energized state of the membrane is not a specific feature of succinate oxidation, as proposed in the literature, since it was also observed in a mutant of B. subtilis lacking succinate:quinone reductase as well as for substrates other than succinate. Possible mechanisms of the energy-dependent regulation of menaquinone-dependent respiration in B. subtilis are discussed.

* Corresponding author. Mailing address: A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Vorobjovy Gory, 119992 Moscow, Russia. Phone: (7) (095) 939-55-49. Fax: (7) (095) 939-03-38. E-mail: konst{at}genebee.msu.su.

Journal of Bacteriology, October 2002, p. 5339-5347, Vol. 184, No. 19
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.19.5339-5347.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Mustafa, G., Migita, C. T., Ishikawa, Y., Kobayashi, K., Tagawa, S., Yamada, M. (2008). Menaquinone as Well as Ubiquinone as a Bound Quinone Crucial for Catalytic Activity and Intramolecular Electron Transfer in Escherichia coli Membrane-bound Glucose Dehydrogenase. J. Biol. Chem. 283: 28169-28175 [Abstract] [Full Text]  
  • Fuchs, U., Manns, I., Steinberg, G. (2005). Microtubules Are Dispensable for the Initial Pathogenic Development but Required for Long-Distance Hyphal Growth in the Corn Smut Fungus Ustilago maydis. Mol. Biol. Cell 16: 2746-2758 [Abstract] [Full Text]  
  • Weber, I., Gruber, C., Steinberg, G. (2003). A Class-V Myosin Required for Mating, Hyphal Growth, and Pathogenicity in the Dimorphic Plant Pathogen Ustilago maydis. Plant Cell 15: 2826-2842 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»