The transition metal binding properties of a 3RD generation bleomycin analogue, tallysomycin

Frederick T. Greenaway; James C. Dabrowiak; Mark Van Husen; Robert Grulich; Stanley T. Crooke

doi:10.1016/0006-291X(78)91160-9

The transition metal binding properties of a 3RD generation bleomycin analogue, tallysomycin

Frederick T. Greenaway, James C. Dabrowiak, Mark Van Husen, Robert Grulich, Stanley T. Crooke

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

Abstract

Employing a number of physical techniques the transition metal binding site of the bleomycin (BLM) related antibiotic tallysomycin (TLM) has been determined. The new antibiotic was shown to have two metal binding sites. One site is similar to that of bleomycin and involves the pyrimidine-imidazole portion of the molecule. The second binding site, which is thermodynamically less stable than the first site, utilizes the amino group of the L-talose moiety and the amino groups located in the β lysine-spermidine portion of the antibiotic. The presence of two metal binding sites and its implication on the mechanism of action of TLM is also discussed.

Original language	English (US)
Pages (from-to)	1407-1414
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	85
Issue number	4
DOIs	https://doi.org/10.1016/0006-291X(78)91160-9
State	Published - Dec 29 1978

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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abstract = "Employing a number of physical techniques the transition metal binding site of the bleomycin (BLM) related antibiotic tallysomycin (TLM) has been determined. The new antibiotic was shown to have two metal binding sites. One site is similar to that of bleomycin and involves the pyrimidine-imidazole portion of the molecule. The second binding site, which is thermodynamically less stable than the first site, utilizes the amino group of the L-talose moiety and the amino groups located in the β lysine-spermidine portion of the antibiotic. The presence of two metal binding sites and its implication on the mechanism of action of TLM is also discussed.",

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AU - Van Husen, Mark

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AU - Crooke, Stanley T.

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AB - Employing a number of physical techniques the transition metal binding site of the bleomycin (BLM) related antibiotic tallysomycin (TLM) has been determined. The new antibiotic was shown to have two metal binding sites. One site is similar to that of bleomycin and involves the pyrimidine-imidazole portion of the molecule. The second binding site, which is thermodynamically less stable than the first site, utilizes the amino group of the L-talose moiety and the amino groups located in the β lysine-spermidine portion of the antibiotic. The presence of two metal binding sites and its implication on the mechanism of action of TLM is also discussed.

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The transition metal binding properties of a 3RD generation bleomycin analogue, tallysomycin

Abstract

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