Spectral shifts of cytochrome c oxidase induced by complexons

Alexander Konstantinov, Tatiana Vygodina, Eugenia Popova, Vladimir Berka, Andrey Musatov

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Ca2+-chelating agents, such as EDTA and ATP, are shown to bring about a rapid spectral response of the oxidized cytochrome c oxidase due to reversal of the Ca2+-induced red shift of the γ- and α-absorption bands of the ferric enzyme. In addition, complexons are found to bring about Ca2+-independent, slow irreversible spectral changes indicative of a conformational transition of cytochrome oxidase. 1 mol EDTA per mol enzyme is sufficient to produce the maximal effect even in the presence of excess Ca2+, indicating high specificity of interaction. It is suggested that the conformation of cytochrome c oxidase may be regulated by the tightly bound 'non-redox' metal ions (Mg, Zn, Cux) known to be present in the enzyme. These ions might be involved in specific binding of physiological effectors with chelating properties, such as ATP.

Original languageEnglish (US)
Pages (from-to)39-42
Number of pages4
JournalFEBS Letters
Volume245
Issue number1-2
DOIs
StatePublished - Mar 13 1989
Externally publishedYes

Keywords

  • ATP
  • Complexon
  • Conformational change
  • Cytochrome-c oxidase
  • Metal ion binding
  • Spectral shift

ASJC Scopus subject areas

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

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