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- Title
Structural characterization of the P<sub>CO/O2</sub> oxidase.
- Authors
Hong Ji; Syun-RuYeh; Rousseau, Denis L.
- Abstract
The structural properties of a key transient oxygen intermediate of cytochrome c oxidase, PR, remain an enigma, although inferences have been drawn from its equilibrium analogues, , PH and PM. With resonance Raman spectroscopy, an oxygen isotope-sensitive band at 806cm−1 was observed in PCO/O2 produced by adding CO and O2 to the resting enzyme. The vibrational band shifted to 771cm−1 upon isotopic substitution of 16O2 with 18O2. The same modes at 806 and 771cm−1 were present simultaneously when the mixed isotope, 18O16O, was employed, indicating that in the O–O bond is cleaved, resulting in a Fe4+ O2− structure. This result unifies the nature of the three equilibrium analogues of the PR intermediate.
- Subjects
PHOTOSYNTHETIC oxygen evolution; CYTOCHROMES; RAMAN spectroscopy; ENZYMES
- Publication
FEBS Letters, 2005, Vol 579, Issue 28, p6361
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2005.10.018