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
        }
}
View on PubMed
doi.org
39 Citations
Highly Influential Citations
1
Background Citations
2

Figures from this paper

39 Citations

Active site intermediates in the reduction of O(2) by cytochrome oxidase, and their derivatives.

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.

Structural characterization of the PCO/O2 compound of cytochrome c oxidase

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.

Resonance Raman spectroscopy of oxoiron(IV) porphyrin pi-cation radical and oxoiron(IV) hemes in peroxidase intermediates.

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.

An oxo‐ferryl tryptophan radical catalytic intermediate in cytochrome c and quinol oxidases trapped by microsecond freeze‐hyperquenching (MHQ)

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.

References

SHOWING 1-10 OF 26 REFERENCES

Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase.

This work proposes a mechanism for O---O bond cleavage that proceeds by concerted hydrogen atom transfer from the cross-linked His---Tyr species to produce the product oxoferryl species, CuB2+---OH-, and the tyrosyl radical.

Time Dependence of the Catalytic Intermediates in Cytochromec Oxidase*

A comparison of the change in the spin equilibrium with the formation of the hydroxy intermediate demonstrates that this intermediate is high spin, and this intermediate does not build up a sufficient population to be detected because its decay rate is too fast in buffered H2O at neutral pH.

Time-resolved resonance Raman elucidation of the pathway for dioxygen reduction by cytochrome c oxidase

Time-resolved resonance Raman (RR) spectra were observed for catalytic intermediates of bovine cytochrome c oxidase at room temperature by using an Artificial Cardiovascular System for Enzymatic…

The intrinsic stability of the second intermediate following the dioxygen‐bound form in the O2 reduction by cytochrome c oxidase

Selective resonance Raman observation of the "607 nm" form generated in the reaction of oxidized cytochrome c oxidase with hydrogen peroxide.

The interaction of cytochrome oxidase with hydrogen peroxide: the relationship of compounds P and F.

It is suggested that compound F is a hydrogen peroxide adduct of Cytochrome oxidase with cytochrome a3 in the low-spin state and that compound P is an oxyferryl state of cy tochrome alpha 3 in support of the recent Raman data of Proshlyakov et al.

Time-Resolved Resonance Raman Evidence for Tight Coupling between Electron Transfer and Proton Pumping of Cytochrome c Oxidase upon the Change from the FeV Oxidation Level to the FeIV Oxidation Level

The mechanism of dioxygen reduction catalyzed by cytochrome c oxidase, the terminal enzyme of the respiration chain of aerobic organisms, has been investigated with time-resolved resonance Raman…

Resonance Raman spectra of highly oxidized metalloporphyrins and heme proteins

Resonance Raman examination of axial ligand bonding and spin-state equilibria in metmyoglobin hydroxide and other heme derivatives.

Raman frequency shifts are used to estimate differences in bond strain energies between MbIIIX and HbIIIX (X = OH-, F-).

Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase.

Crystal structures of bovine heart cytochrome c oxidase in the fully oxidized, fully reduced, azide-bound, and carbon monoxide-bound states were determined at 2.35, 2.9, and 2.8 angstrom resolution, indicating the aspartate as the as partate pumping site for the O2 reduction by the enzyme.