Escherichia coli has several elaborate sensing mechanisms for response to the availability of oxygen and the presence of other electron acceptors. The adaptive responses are coordinated by a group of global regulators, which include the one-component Fnr protein, and the two-component Arc system. To quantitate the contribution of Arc and Fnr-dependent regulation in catabolism, arcA and fnr mutant strains were constructed using the recently developed lambda derived recombination system. The metabolic activity of wildtype E. coli, an arcA mutant, an fnr mutant, and a double arcA-fnr mutant, via the fermentative pathways in glucose-limited cultures and different oxygen concentrations was studied in chemostat cultures at steady state. It was found that the most significant role of ArcA is under microaerobic conditions, while that of FNR is under more strictly anaerobic conditions. The FNR protein is normally inactive during microaerobic conditions. However, our results indicate that in the arcA mutant strain the cells behave as if a higher level of the FNR regulator is in the activated form compared to the wildtype strain during the transition from aerobic to microanaerobic growth. The results show a significant increase in the flux through pyruvate formate lyase (PFL) in the presence of oxygen. The activity of FNR-regulated pathways in the arcA mutant strain is correlated with the high redox potential obtained under microaerobic growth.

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