Abstract
Cu(I) and Cu(II) form stable 1:1 complexes with bleomycin (BLM). The affinity of both metals for the drug is greater than that of Fe(II). Cu(I)-BLM A2 binds to calf thymus DNA with about the same affinity as Fe(II)-BLM, as judged by DNA-induced fluorescence quenching of the bithiazole moiety of BLM. Based on 1H NMR and potentiometric titration data, the Cu(I) complexes of BLM are shown to have geometries very different than those of other BLM-metal(II) complexes studied thus far. As Cu(I)-BLM is oxidation-reduction active, its geometry is of importance in defining the structural requirements for BLM activity.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1514-1517 |
| Number of pages | 4 |
| Journal | Journal of Biological Chemistry |
| Volume | 256 |
| Issue number | 4 |
| State | Published - 1981 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Copper(I)-bleomycin. A structurally unique oxidation-reduction active complex. / Oppenheimer, N. J.; Chang, C.; Rodriguez, L. O.; Hecht, Sidney.
In: Journal of Biological Chemistry, Vol. 256, No. 4, 1981, p. 1514-1517.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Copper(I)-bleomycin. A structurally unique oxidation-reduction active complex
AU - Oppenheimer, N. J.
AU - Chang, C.
AU - Rodriguez, L. O.
AU - Hecht, Sidney
PY - 1981
Y1 - 1981
N2 - Cu(I) and Cu(II) form stable 1:1 complexes with bleomycin (BLM). The affinity of both metals for the drug is greater than that of Fe(II). Cu(I)-BLM A2 binds to calf thymus DNA with about the same affinity as Fe(II)-BLM, as judged by DNA-induced fluorescence quenching of the bithiazole moiety of BLM. Based on 1H NMR and potentiometric titration data, the Cu(I) complexes of BLM are shown to have geometries very different than those of other BLM-metal(II) complexes studied thus far. As Cu(I)-BLM is oxidation-reduction active, its geometry is of importance in defining the structural requirements for BLM activity.
AB - Cu(I) and Cu(II) form stable 1:1 complexes with bleomycin (BLM). The affinity of both metals for the drug is greater than that of Fe(II). Cu(I)-BLM A2 binds to calf thymus DNA with about the same affinity as Fe(II)-BLM, as judged by DNA-induced fluorescence quenching of the bithiazole moiety of BLM. Based on 1H NMR and potentiometric titration data, the Cu(I) complexes of BLM are shown to have geometries very different than those of other BLM-metal(II) complexes studied thus far. As Cu(I)-BLM is oxidation-reduction active, its geometry is of importance in defining the structural requirements for BLM activity.
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UR - http://www.scopus.com/inward/citedby.url?scp=0019473707&partnerID=8YFLogxK
M3 - Article
C2 - 6161924
AN - SCOPUS:0019473707
VL - 256
SP - 1514
EP - 1517
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 4
ER -