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The transfer of iron between ceruloplasmin and transferrins.

Kenneth N White | Celia Conesa | Lourdes Sánchez | Maryam Amini | Sebastien Farnaud | Chanakan Lorvoralak | Robert W Evans
Biochimica et biophysica acta | 2012

It is over 60years since the discovery and isolation of the serum ferroxidase ceruloplasmin. In that time much basic information about the protein has been elucidated including its catalytic and kinetic properties as an enzyme, expression, sequence and structure. The importance of its biological role is indicated in genetic diseases such as aceruloplasminemia where its function is lost through mutation. Despite this wealth of data, fundamental questions about its action remain unanswered and in this article we address the question of how ferric iron produced by the ferroxidase activity of ceruloplasmin could be taken up by transferrins or lactoferrins.

Pubmed ID: 22040722

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Jmol (tool)

RRID:SCR_003796

An open-source Java viewer for chemical structures in 3D with features for chemicals, crystals, materials and biomolecules. It is cross-platform, running on Windows, Mac OS X, and Linux/Unix systems and features an applet, application, and systems integration component.

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