Cytochrome b558 monitors the steady state redox state of the ubiquinone pool in the aerobic respiratory chain of Escherichia coli.

@article{Lorence1987CytochromeBM,
  title={Cytochrome b558 monitors the steady state redox state of the ubiquinone pool in the aerobic respiratory chain of Escherichia coli.},
  author={Robert M. Lorence and Katharine C. Carter and Greenwood Green and Robert B Gennis},
  journal={The Journal of biological chemistry},
  year={1987},
  volume={262 22},
  pages={10532-6}
}
The aerobic respiratory chain of Escherichia coli contains two terminal oxidases, the cytochrome o complex and the cytochrome d complex. These both function as ubiquinol-8 oxidases and reduce molecular oxygen to water. Electron flux is funneled from a variety of dehydrogenases, such as succinate dehydrogenase, through ubiquinone-8, to either of the terminal oxidases. A strain was examined which lacks the intact cytochrome d complex, but which overproduces one of the two subunits of this complex… CONTINUE READING

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