Abstract
The reaction of peroxide with cytochrome oxidase generates a peroxide compound having a Soret maximum at 428 nm. X-ray absorption spectroscopy analysis of the local structure of the active site iron shows marked similarity to that of the cytochrome c peroxidase intermediate Compound ES, which contains a short iron to proximal nitrogen distance compared to globins. Reductive titration of the 580 nm band of this compound indicates that the iron is one oxidizing equivalent above the resting oxidized form. These results support the presence of a ferryl iron (Fe(IV) = O) in the peroxide compound similar to that found for the peroxidases.
Original language | English (US) |
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Pages (from-to) | 7159-7163 |
Number of pages | 5 |
Journal | The Journal of biological chemistry |
Volume | 263 |
Issue number | 15 |
State | Published - May 25 1988 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology