Resonance Raman characterization of the P intermediate in the reaction of bovine cytochrome c oxidase.

@article{Ogura2004ResonanceRC,
  title={Resonance Raman characterization of the P intermediate in the reaction of bovine cytochrome c oxidase.},
  author={Takashi Ogura and Teizo Kitagawa},
  journal={Biochimica et biophysica acta},
  year={2004},
  volume={1655 1-3},
  pages={
          290-7
        }
}

Figures from this paper

Respiratory conservation of energy with dioxygen: cytochrome C oxidase.

X-ray structures of bovine CcO in different oxidation and ligand binding states showed that the O₂reduction site, which is composed of Fe (heme a 3) and Cu (CuB), drives a non-sequential four-electron transfer for reduction of O ₂to water without releasing any reactive oxygen species.

Interconversions of P and F intermediates of cytochrome c oxidase from Paracoccus denitrificans

It is demonstrated that the artificial F state, classically generated by reaction with an excess of hydrogen peroxide, can be converted into a new P state by addition of ammonia at pH 9.5, and suggested that ammonia coordinates directly to CuB in the binuclear active center in this P state.

Kinetic Resolution of a Tryptophan-radical Intermediate in the Reaction Cycle of Paracoccus denitrificans Cytochrome c Oxidase*

Findings show that Trp-272 is a redox-active residue and is in this respect on an equal par to the metallocenters of the cytochrome c oxidase.

Cryo-EM structures of intermediates suggest an alternative catalytic reaction cycle for cytochrome c oxidase

The results suggest that in the O-state the active site contains a peroxide dianion and in the P-state possibly an intact dioxygen molecule, the F-state may contain a superoxide anion, and the enzyme’s catalytic cycle may have to be turned by 180 degrees.

A Water Dimer Shift Activates a Proton Pumping Pathway in the PR → F Transition of ba3 Cytochrome c Oxidase.

The calculations show that the movement of the H2O molecules in the DNC affects the pKa values of the residue side chains of Tyr237 and His376+, which are crucial for proton transfer/pumping in ba3 CcO from Tt.

Redox-induced Protein Structural Changes in Cytochrome bo Revealed by Fourier Transform Infrared Spectroscopy and [13C]Tyr Labeling*

Redox-induced main chain changes at a Tyr residue(s) are associated with structural changes at Glu-286 near the binuclear metal centers and may be related to switching of the K-channel operative at the reductive phase to D-channel at the oxidative phase of the dioxygen reduction cycle via conformational changes in the middle of helix VI.

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