Open AccessTransmembrane pH of Clostridium acetobutylicum is inverted (more acidic inside) when the in vivo activity of hydrogenase is decreased
Author(s) -
Laurence Girbal,
I. Vasconcelos,
Philippe Soucaille
Publication year - 1994
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.176.19.6146-6147.1994
Subject(s) - clostridium acetobutylicum , hydrogenase , biology , in vivo , biochemistry , cytoplasm , transmembrane protein , chemiosmosis , biophysics , intracellular , electrochemical gradient , clostridium , intracellular ph , enzyme , bacteria , membrane , atp synthase , butanol , genetics , receptor , microbiology and biotechnology , ethanol
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.