A comparative EPR investigation of the multicopper proteins nitrous-oxide reductase and cytochrome c oxidase.

@article{Antholine1992ACE,
  title={A comparative EPR investigation of the multicopper proteins nitrous-oxide reductase and cytochrome c oxidase.},
  author={W. Antholine and D. Kastrau and G. Steffens and G. Buse and W. Zumft and P. Kroneck},
  journal={European journal of biochemistry},
  year={1992},
  volume={209 3},
  pages={
          875-81
        }
}
The multicopper proteins, nitrous-oxide reductase (N2OR) and cytochrome c oxidase (COX), were investigated by EPR spectroscopy at microwave frequencies 2.4-35 GHz. Our results support a Cu-Cu interaction in COX and N2OR. At least 10 lines in the 2.7-GHz, 12 lines in the 4.6-GHz and 14 lines in the 9.2 GHz spectra were resolved for N2OR. Eight copper lines at 2.7 GHz, about nine lines at 4.6 GHz and about six lines at 9.2 GHz were resolved for COX. Simulations of the EPR spectra were consistent… Expand
View on PubMed
doi.org
121 Citations
Highly Influential Citations
3
Background Citations
9
Methods Citations
3

Topics from this paper

      121 Citations

      Citation Type

      Citation Type

      Walking the seven lines: binuclear copper A in cytochrome c oxidase and nitrous oxide reductase
      • P. Kroneck
      • Chemistry, Medicine
      • JBIC Journal of Biological Inorganic Chemistry
      • 2017
      • 15
      CuA and CuZ are variants of the electron transfer center in nitrous oxide reductase.
      • 36
      • PDF
      Perturbation of the CuA site in cytochrome-c oxidase of Paracoccus denitrificans by replacement of Met227 with isoleucine.
      • 27
      Multiple forms of the catalytic centre, CuZ, in the enzyme nitrous oxide reductase from Paracoccus pantotrophus.
      • 59
      • PDF
      Spectroscopic and mutagenesis studies on the CuA centre from the cytochrome-c oxidase complex of Paracoccus denitrificans.
      • 41
      The tetranuclear copper active site of nitrous oxide reductase: the CuZ center
      • 29
      • PDF
      The Electron Transfer Complex between Cytochrome c552 and the CuA Domain of the Thermus thermophilus ba3 Oxidase
      • 36
      • PDF
      Binuclear Copper A
      • 4
      The CuA site of cytochrome c oxidase
      • 7
      Electronic structures of the Cu2S2 core of the CuA site in cytochrome c oxidase and nitrous oxide reductase
      • 6
      ...
      1
      2
      3
      4
      5
      ...

      References

      SHOWING 1-10 OF 50 REFERENCES
      Multiple frequency EPR studies on three forms of oxidized cytochrome c oxidase.
      • 16
      • PDF
      An EPR study of the lineshape of copper in cytochrome c oxidase.
      • 32
      A model of the copper centres of nitrous oxide reductase (Pseudomonas stutzeri)
      • 90
      Multifrequency EPR evidence for a bimetallic center at the CuA site in cytochrome c oxidase
      • 102
      The cupric site in nitrous oxide reductase contains a mixed‐valence [Cu(II),Cu(I)] binuclear center: A multifrequency electron paramagnetic resonance investigation
      • 153
      The nature of the cupric site in nitrous oxide reductase and of CuA in cytochrome c oxidase
      • 49
      On the nature of cysteine coordination to CuA in cytochrome c oxidase.
      • 42
      • PDF
      Cytochrome c oxidase is a three-copper, two-heme-A protein.
      • 139
      Pseudomonas stutzeri N2O reductase contains CuA-type sites.
      • 69
      • PDF
      Properties of a copper-containing cytochrome ba3: a second terminal oxidase from the extreme thermophile Thermus thermophilus.
      • 103
      • PDF
      ...
      1
      2
      3
      4
      5
      ...