An Escherichia coli mutant quinol:fumarate reductase contains an EPR-detectable semiquinone stabilized at the proximal quinone-binding site.

@article{Hgerhll1999AnEC,
  title={An Escherichia coli mutant quinol:fumarate reductase contains an EPR-detectable semiquinone stabilized at the proximal quinone-binding site.},
  author={Cecilia H{\"a}gerh{\"a}ll and Sergey G Magnitsky and Vladimir D Sled and Imke Schr{\"o}der and Robert P. Gunsalus and Gary Cecchini and Tomoko Ohnishi},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 37},
  pages={26157-64}
}
The EPR and thermodynamic properties of semiquinone (SQ) species stabilized by mammalian succinate:quinone reductase (SQR) in situ in the mitochondrial membrane and in the isolated enzyme have been well documented. The equivalent semiquinones in bacterial membranes have not yet been characterized, either in SQR or quinol:fumarate reductase (QFR) in situ. In this work, we describe an EPR-detectable QFR semiquinone using Escherichia coli mutant QFR (FrdC E29L) and the wild-type enzyme. The SQ… CONTINUE READING

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On the Structure and Function of Succinate: Quinone Oxidoreductase Using Bacillus subtilis as a Model Organism

C. Hägerhäll
Ph.D. thesis, • 1994
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