PMID:21987791
| Citation |
Borisov, VB, Murali, R, Verkhovskaya, ML, Bloch, DA, Han, H, Gennis, RB and Verkhovsky, MI (2011) Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode. Proc. Natl. Acad. Sci. U.S.A. 108:17320-4 |
|---|---|
| Abstract |
Escherichia coli is known to couple aerobic respiratory catabolism to ATP synthesis by virtue of the primary generators of the proton motive force-NADH dehydrogenase I, cytochrome bo(3), and cytochrome bd-I. An E. coli mutant deficient in NADH dehydrogenase I, bo(3) and bd-I can, nevertheless, grow aerobically on nonfermentable substrates, although its sole terminal oxidase cytochrome bd-II has been reported to be nonelectrogenic. In the current work, the ability of cytochrome bd-II to generate a proton motive force is reexamined. Absorption and fluorescence spectroscopy and oxygen pulse methods show that in the steady-state, cytochrome bd-II does generate a proton motive force with a H(+)/e(-) ratio of 0.94 ± 0.18. This proton motive force is sufficient to drive ATP synthesis and transport of nutrients. Microsecond time-resolved, single-turnover electrometry shows that the molecular mechanism of generating the proton motive force is identical to that in cytochrome bd-I. The ability to induce cytochrome bd-II biosynthesis allows E. coli to remain energetically competent under a variety of environmental conditions. |
| Links |
PubMed PMC3198357 Online version:10.1073/pnas.1108217108 |
| Keywords |
Adenosine Triphosphate/biosynthesis; Aerobiosis; Cytochromes/metabolism; Electron Transport; Electron Transport Chain Complex Proteins/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins/metabolism; Membrane Potentials; Models, Biological; NAD/metabolism; Oxidoreductases/metabolism; Proton-Motive Force |
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