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 language | English (US) |
|---|---|
| Pages (from-to) | 14-21 |
| Number of pages | 8 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 193 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1 1979 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
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Ruthenium red as a resonance Raman probe of Ca2+ binding sites in biological materials. / Friedman, J. M.; Rousseau, D. L.; Navon, G.; Rosenfeld, Steven; Glynn, P.; Lyons, K. B.
In: Archives of Biochemistry and Biophysics, Vol. 193, No. 1, 01.01.1979, p. 14-21.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Ruthenium red as a resonance Raman probe of Ca2+ binding sites in biological materials
AU - Friedman, J. M.
AU - Rousseau, D. L.
AU - Navon, G.
AU - Rosenfeld, Steven
AU - Glynn, P.
AU - Lyons, K. B.
PY - 1979/1/1
Y1 - 1979/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0018451747&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0018451747&partnerID=8YFLogxK
U2 - 10.1016/0003-9861(79)90002-X
DO - 10.1016/0003-9861(79)90002-X
M3 - Article
C2 - 222215
AN - SCOPUS:0018451747
VL - 193
SP - 14
EP - 21
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 1
ER -