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The X-ray structure of human serum ceruloplasmin at 3.1.Å: nature of the copper centres

Zaitseva, Irina, Zaitsev, Vjacheslav, Card, Graeme, Moshkov, Kirill, Bax, Benjamin, Ralph, Adam and Lindley, Peter 1996. The X-ray structure of human serum ceruloplasmin at 3.1.Å: nature of the copper centres. JBIC Journal of Biological Inorganic Chemistry 1 (1) , pp. 15-23. 10.1007/s007750050018

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Abstract

The X-ray structure of human serum ceruloplasmin has been solved at a resolution of 3.1 Å. The structure reveals that the molecule is comprised of six plastocyanin-type domains arranged in a triangular array. There are six copper atoms; three form a trinuclear cluster sited at the interface of domains 1 and 6, and there are three mononuclear sites in domains 2, 4 and 6. Each of the mononuclear coppers is coordinated to a cysteine and two histidine residues, and those in domains 4 and 6 also coordinate to a methionine residue; in domain 2, the methionine is replaced by a leucine residue which may form van der Waals type contacts with the copper. The trinuclear centre and the mononuclear copper in domain 6 form a cluster essentially the same as that found in ascorbate oxidase, strongly suggesting an oxidase role for ceruloplasmin in the plasma.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: Springer
ISSN: 0949-8257
Last Modified: 06 Jul 2018 10:56
URI: http://orca.cardiff.ac.uk/id/eprint/112645

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