Journal of Bacteriology, September 2000, p. 4934-4940, Vol. 182, No. 17
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
EC Slater Institute, University of Amsterdam, 1018 WS Amsterdam, The Netherlands,1 and Department of Molecular Microbiology, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, United Kingdom2
Received 1 December 1999/Accepted 6 June 2000
The capacity of Escherichia coli to adapt its
catabolism to prevailing redox conditions resides mainly in three
catabolic branch points involving (i) pyruvate formate-lyase (PFL) and
the pyruvate dehydrogenase complex (PDHc), (ii) the exclusively
fermentative enzymes and those of the Krebs cycle, and (iii) the
alternative terminal cytochrome bd and
cytochrome bo oxidases. A quantitative analysis of the
relative catabolic fluxes through these pathways is presented for
steady-state glucose-limited chemostat cultures with controlled oxygen
availability ranging from full aerobiosis to complete
anaerobiosis. Remarkably, PFL contributed significantly to the
catabolic flux under microaerobic conditions and was found to be
active simultaneously with PDHc and cytochrome bd
oxidase-dependent respiration. The synthesis of PFL and cytochrome
bd oxidase was found to be maximal in
the lower microaerobic range but not in a
ArcA mutant, and we
conclude that the Arc system is more active with respect to
regulation of these two positively regulated operons during
microaerobiosis than during anaerobiosis.
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