Electron transfer to the active site of the bacterial nitric oxide reductase is controlled by ligand binding to heme b₃.

@article{Field2011ElectronTT,
  title={Electron transfer to the active site of the bacterial nitric oxide reductase is controlled by ligand binding to heme b₃.},
  author={Sarah J. Field and M Dolores Rold{\'a}n and Sophie J. Marritt and Julea N Butt and D. J. Richardson and Nicholas J. Watmough},
  journal={Biochimica et biophysica acta},
  year={2011},
  volume={1807 4},
  pages={451-7}
}
The active site of the bacterial nitric oxide reductase from Paracoccus denitrificans contains a dinuclear centre comprising heme b₃ and non heme iron (Fe(B)). These metal centres are shown to be at isopotential with midpoint reduction potentials of E(m) ≈ +80 mV. The midpoint reduction potentials of the other two metal centres in the enzyme, heme c and heme b, are greater than the dinuclear centre suggesting that they act as an electron receiving/storage module. Reduction of the low-spin heme… CONTINUE READING

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