X-ray structure of the zinc complex of the central metal chelation site of the antitumour drug streptonigrin

Georgina V. Long; Margaret M. Harding; Peter Turner

doi:10.1016/S0277-5387(00)00352-1

X-ray structure of the zinc complex of the central metal chelation site of the antitumour drug streptonigrin

Georgina V. Long, Margaret M. Harding^*, Peter Turner

^*Corresponding author for this work

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

9 Citations (Scopus)

Abstract

The X-ray structure of the 1:1 complex between zinc(II) triflate and 3-amino-6,6'-bis(methoxycarbonyl)-2,2'-bipyridine is reported. This ligand contains the central chelation site present in the DNA-binding antitumour antibiotic streptonigrin. The complex is distorted octahedral involving the 2,2'-bipyridyl site and the carbonyl groups at the 6,6'-positions as well as two axial water molecules. The structure confirms that formation of similar complexes with streptonigrin is possible. (C) 2000 Elsevier Science Ltd.

Original language	English
Pages (from-to)	1067-1071
Number of pages	5
Journal	Polyhedron
Volume	19
Issue number	9
DOIs	https://doi.org/10.1016/S0277-5387(00)00352-1
Publication status	Published - 15 May 2000
Externally published	Yes

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@article{b6aa67077dce4684bf79b97268768288,

title = "X-ray structure of the zinc complex of the central metal chelation site of the antitumour drug streptonigrin",

abstract = "The X-ray structure of the 1:1 complex between zinc(II) triflate and 3-amino-6,6'-bis(methoxycarbonyl)-2,2'-bipyridine is reported. This ligand contains the central chelation site present in the DNA-binding antitumour antibiotic streptonigrin. The complex is distorted octahedral involving the 2,2'-bipyridyl site and the carbonyl groups at the 6,6'-positions as well as two axial water molecules. The structure confirms that formation of similar complexes with streptonigrin is possible. (C) 2000 Elsevier Science Ltd.",

keywords = "2,2'-Bipyridyl, 6,6'-Dicarboxy-2,2'-bipyridyl, Antitumour, Streptonigrin, Zinc",

author = "Long, \{Georgina V.\} and Harding, \{Margaret M.\} and Peter Turner",

year = "2000",

month = may,

day = "15",

doi = "10.1016/S0277-5387(00)00352-1",

language = "English",

volume = "19",

pages = "1067--1071",

journal = "Polyhedron",

issn = "0277-5387",

publisher = "Elsevier Ltd.",

number = "9",

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TY - JOUR

T1 - X-ray structure of the zinc complex of the central metal chelation site of the antitumour drug streptonigrin

AU - Long, Georgina V.

AU - Harding, Margaret M.

AU - Turner, Peter

PY - 2000/5/15

Y1 - 2000/5/15

N2 - The X-ray structure of the 1:1 complex between zinc(II) triflate and 3-amino-6,6'-bis(methoxycarbonyl)-2,2'-bipyridine is reported. This ligand contains the central chelation site present in the DNA-binding antitumour antibiotic streptonigrin. The complex is distorted octahedral involving the 2,2'-bipyridyl site and the carbonyl groups at the 6,6'-positions as well as two axial water molecules. The structure confirms that formation of similar complexes with streptonigrin is possible. (C) 2000 Elsevier Science Ltd.

AB - The X-ray structure of the 1:1 complex between zinc(II) triflate and 3-amino-6,6'-bis(methoxycarbonyl)-2,2'-bipyridine is reported. This ligand contains the central chelation site present in the DNA-binding antitumour antibiotic streptonigrin. The complex is distorted octahedral involving the 2,2'-bipyridyl site and the carbonyl groups at the 6,6'-positions as well as two axial water molecules. The structure confirms that formation of similar complexes with streptonigrin is possible. (C) 2000 Elsevier Science Ltd.

KW - 2,2'-Bipyridyl

KW - 6,6'-Dicarboxy-2,2'-bipyridyl

KW - Antitumour

KW - Streptonigrin

KW - Zinc

UR - https://www.scopus.com/pages/publications/0034656817

U2 - 10.1016/S0277-5387(00)00352-1

DO - 10.1016/S0277-5387(00)00352-1

M3 - Article

SN - 0277-5387

VL - 19

SP - 1067

EP - 1071

JO - Polyhedron

JF - Polyhedron

IS - 9

ER -

X-ray structure of the zinc complex of the central metal chelation site of the antitumour drug streptonigrin

Abstract

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