A spectroscopic investigation of the metal binding site of bleomycin A2. The Cu(II) and Zn(II) derivatives

James C. Dabrowiak; Frederick T. Greenaway; Walter E. Longo; Mark Van Husen; Stanley T. Crooke

doi:10.1016/0005-2787(78)90218-6

A spectroscopic investigation of the metal binding site of bleomycin A₂. The Cu(II) and Zn(II) derivatives

James C. Dabrowiak, Frederick T. Greenaway, Walter E. Longo, Mark Van Husen, Stanley T. Crooke

Department of Chemistry

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

90 Scopus citations

Abstract

Using a combination of ultraviolet-visible absorption, ¹H NMR and ESR techniques we have established that N(1) of the imidazole and N(1) of the pyrimidine residues of bleomycin A₂ bind to Cu(II) and Zn(II). These observations coupled with the earlier results that the α-amino group of the α-amino carboxamide function and the carbamoyl moiety are also Cu(II)-ligating groups makes it possible to reconstruct the detailed geometry and stereochemistry of the metal binding site of bleomycin A₂.

Original language	English (US)
Pages (from-to)	517-526
Number of pages	10
Journal	BBA Section Nucleic Acids And Protein Synthesis
Volume	517
Issue number	2
DOIs	https://doi.org/10.1016/0005-2787(78)90218-6
State	Published - Feb 16 1978

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General Medicine

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abstract = "Using a combination of ultraviolet-visible absorption, 1H NMR and ESR techniques we have established that N(1) of the imidazole and N(1) of the pyrimidine residues of bleomycin A2 bind to Cu(II) and Zn(II). These observations coupled with the earlier results that the α-amino group of the α-amino carboxamide function and the carbamoyl moiety are also Cu(II)-ligating groups makes it possible to reconstruct the detailed geometry and stereochemistry of the metal binding site of bleomycin A2.",

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AU - Van Husen, Mark

AU - Crooke, Stanley T.

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AB - Using a combination of ultraviolet-visible absorption, 1H NMR and ESR techniques we have established that N(1) of the imidazole and N(1) of the pyrimidine residues of bleomycin A2 bind to Cu(II) and Zn(II). These observations coupled with the earlier results that the α-amino group of the α-amino carboxamide function and the carbamoyl moiety are also Cu(II)-ligating groups makes it possible to reconstruct the detailed geometry and stereochemistry of the metal binding site of bleomycin A2.

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A spectroscopic investigation of the metal binding site of bleomycin A₂. The Cu(II) and Zn(II) derivatives

Abstract

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