Transmembrane pH of Clostridium acetobutylicum is inverted (more acidic inside) when the in vivo activity of hydrogenase is decreased

Author:

Girbal L1,Vasconcelos I1,Soucaille P1

Affiliation:

1. Centre de Ingénierie Gilbert Durand, Institut National des Sciences Appliquées, Toulouse, France.

Abstract

Evidence is reported here that alkalinization of Clostridium acetobutylicum cytoplasm involves hydrogenase activity. A decrease of in vivo hydrogenase activity is accompanied by intracellular accumulation of protons leading to a negative (interior acidic) pH gradient. However, the organism is able to maintain a constant proton motive force by interconverting chemical and electrical potentials.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference14 articles.

1. Adams , M. W. W. , L. E. Mortenson , and J. S. Chen . 1981 . Hydrogenase. Biochim. Biophys. Acta 594 : 105 - 176 .

2. Interconversion of components of the bacterial proton motive force by electrogenic potassium transport;Bakker E. P.;J. Bacteriol.,1981

3. Reduced coenzyme F420: heterodisulfide oxidoreductase, a proton-translocating redox system in methanogenic bacteria;Deppenmeier U.;Proc. Natl. Acad. Sci. USA,1990

4. Girbal L L Vasconcelos and P. Soucaille. How neutral red modified carbon and electron flow in Clostidium acetobutylicum grown in chemostat culture at neutral pH. FEMS Microbiol. Rev. in press.

5. Electron transport and electrochemical proton gradient in membrane vesicles of Clostridium thermoautotrophicum;Hugenholtz J.;J. Bacteriol.,1989

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