Conformational change of cytochrome a3 induced by oxidized cytochrome c

Andrey Musatov, Alexander A. Konstantinov

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


Cyanide binding with the oxidized resting Yonetani-type cytochrome c-oxidase followed spectrophotometrically reveals a relatively rapid initial phase the rate of which shows saturation behaviour with respect to [HCN] and secondary slower absorption changes to a first approximation independent of the ligand concentration. Oxidized cytochrome c greatly accelerates the initial phase of cyanide binding but does not affect significantly contribution or rate constant of the slow phase. The same effect is exerted by poly-L-lysine. Within a framework of a reaction mechanism assuming Cu2+B to be the initial HCN-binding site, cytochrome c3+ and other polycations are likely to bring about a conformational change of cytochrome oxidase resulting in an increased affinity of Cu2+B for HCN. This could occur by virtue of loosening a bond between Cu2+B and one of its endogenous ligands facilitating displacement of the latter by HCN.

Original languageEnglish (US)
Pages (from-to)295-299
Number of pages5
JournalFEBS Letters
Issue number2
StatePublished - Oct 10 1988
Externally publishedYes


  • Conformational change
  • Cu-site
  • Cyanide binding
  • Cytochrome c
  • Cytochrome c-oxidase
  • Poly-L-lysine

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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