NDLI: Functional role of the putative iron ligands in the ferroxidase activity of recombinant human hephaestin.

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Functional role of the putative iron ligands in the ferroxidase activity of recombinant human hephaestin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Vashchenko, Ganna Macgillivray, Ross T. A.
Description	Country affiliation: Canada Author Affiliation: Vashchenko G ( Department of Biochemistry and Molecular Biology, Centre for Blood Research, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, V6T1Z3, Canada.)
Abstract	Hephaestin is a multicopper ferroxidase expressed mainly in the mammalian small intestine. The ferroxidase activity of hephaestin is thought to play an important role during iron export from intestinal enterocytes and the subsequent iron loading of the blood protein transferrin, which delivers iron to the tissues. Structurally, the ectodomain of hephaestin is predicted to resemble ceruloplasmin, the soluble ferroxidase of blood. In this study, the human hephaestin ectodomain was expressed in baby hamster kidney cells and purified to electrophoretic homogeneity. Ion exchange chromatography of purified recombinant human hephaestin (rhHp) resulted in the isolation of hephaestin fractions with distinct catalytic and spectroscopic properties. The fraction of rhHp with the highest enzymatic activity also showed an enhanced molar absorptivity at 600 nm, characteristic of type 1 copper sites. Kinetic analysis revealed that rhHp possesses both high-affinity and low-affinity binding sites for ferrous iron. To investigate the role of particular residues in iron specificity of hephaestin, mutations of putative iron ligands were introduced into rhHp using site-directed mutagenesis. Kinetic analysis of ferroxidation rates of wild-type rhHp and mutants demonstrated the important roles of hephaestin residues E960 and H965 in the observed ferroxidase activity.
File Format	HTM / HTML
ISSN	09498257
Issue Number	8
Volume Number	17
e-ISSN	14321327
Journal	JBIC Journal of Biological Inorganic Chemistry
Language	English
Publisher	Springer
Publisher Date	2012-12-01
Publisher Place	Germany
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Ceruloplasmin Metabolism Iron Membrane Proteins Cells, Cultured Chemistry Humans Ligands Genetics Mutagenesis, Site-directed Recombinant Proteins Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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