Spectral and kinetic equivalence of oxidized cytochrome c oxidase as isolated and "activated" by reoxidation

Daniel Jancura, Vladimir Berka, Marian Antalik, Jaroslava Bagelova, Robert B. Gennis, Graham Palmer, Marian Fabian

Research output: Contribution to journalArticlepeer-review

Abstract

The spectral and kinetic characteristics of two oxidized states of bovine heart cytochrome c oxidase (CcO) have been compared. The first is the oxidized state of enzyme isolated in the fast form (O) and the second is the form that is obtained immediately after oxidation of fully reduced CcO with O2 (OH). No observable differences were found between O and OH states in: (i) the rate of anaerobic reduction of heme a3 for both the detergent-solubilized enzyme and for enzyme embedded in its natural membraneous environment, (ii) the one-electron distribution between heme a3 and CuB in the course of the full anaerobic reduction, (iii) the optical and (iv) EPR spectra. Within experimental error of these characteristics both forms are identical. Based on these observations it is concluded that the reduction potentials and the ligation states of heme a3 and Cu B are the same for CcO in the O and OH states.

Original languageEnglish (US)
Pages (from-to)30319-30325
Number of pages7
JournalJournal of Biological Chemistry
Volume281
Issue number41
DOIs
StatePublished - Oct 13 2006

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Spectral and kinetic equivalence of oxidized cytochrome c oxidase as isolated and "activated" by reoxidation'. Together they form a unique fingerprint.

Cite this