Journal of Bacteriology · 2000 · 138 citations · 53 references
Life SciencesBiochemistryMicrobiologyBioenergeticsMetabolismMicrobial MetabolismAnaerobic MetabolismBacterial MetabolismCellular RespirationEnergy MetabolismMicrobial RespirationRedox MetabolismAerationBacterial RespirationEscherichia ColiMicroaerobic RespirationPyruvate MetabolismPyruvate OxidationRedox ConditionsTerminal Oxidases
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 delta 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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Mark R. Graef, Svetlana Alexeeva, Jacky L. Snoep et al. · Journal of Bacteriology · 1999 · 324 citations · Full text
Properties of the two terminal oxidases of Escherichia coli
Anne Puustinen, Moshe Finel, Tuomas Haltia et al. · Biochemistry · 1991 · 310 citations
Kiyoshi Kita, Kiyoshi Konishi, Yasutaka Anraku · Journal of Biological Chemistry · 1984 · 273 citations · Full text