Abstract
An earlier stoichiometric analysis of oxygen-limited metabolism of Escherichia coli expressing cloned Vitreoscilla hemoglobin (VHb) suggested improved efficiency of ATP production relative to wild-type controls [Khosla, C., Curtis, J. E., DeModena, J., Rinas, J. & Bailey, J. E. (1990) BioTechnol. 8, 849-853]. This hypothesis has been further examined by determining several energetic parameters of different VHb-expressing E. coli (VHb+) strains relative to controls not expressing VHb (VHb-). The H+/O ratio, the transmembrane delta pH, and the ATP content of VHb+ constructs are 1.5, 1.6 and 2 times, respectively, corresponding values in VHb- controls. VHb was expressed using a low-copy-number vector in E. coli mutant strains lacking cytochrome o, cytochrome d, or both terminal oxidases; significant growth enhancement due to VHb expression was observed only in the strain having functional cytochrome o and lacking cytochrome d. All of these data obtained using different E. coli strains are consistent with a model of VHb action that hypothesizes enhancement by VHb of activity of the lower oxygen-affinity, higher proton-pumping-efficiency cytochrome o terminal oxidase under oxygen-limited growth conditions.
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