Ruthenium red as a resonance Raman probe of Ca2+ binding sites in biological materials

J. M. Friedman, D. L. Rousseau, G. Navon, S. Rosenfeld, P. Glynn, K. B. Lyons

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

We have observed substantial changes in the resonance Raman spectrum of ruthenium red when it is added to calcium ion binding molecules and organelles, including proteins, phospholipids, chelating agents, and intact mitochondria. The addition of Ca2+ ions can reverse these observed spectral changes. In the case of cytochrome c, ruthenium red binding varies with oxidation state in a manner parallel to that for Ca2+ binding. The resonance Raman spectrum of a ruthenium red-phospholipid complex shows differences from that of a ruthenium red-protein complex, enabling us to distinguish between binding to these different classes of molecules. Our studies suggest that the primary constituent of the low-affinity Ca2+ binding sites in mitochondria is cardiolipin.

Original languageEnglish (US)
Pages (from-to)14-21
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume193
Issue number1
DOIs
StatePublished - Mar 1979
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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