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- W2143662073 abstract "Dietary and recycled iron are in the Fe(2+) oxidation state. However, the metal is transported in serum by transferrin as Fe(3+). The multi-copper ferroxidase ceruloplasmin is suspected to be the missing link between acquired Fe(2+) and transported Fe(3+).This study uses the techniques of chemical relaxation and spectrophotometric detection.Under anaerobic conditions, ceruloplasmin captures and oxidizes two Fe(2+). The first uptake occurs in domain 6 (<1ms) at the divalent iron-binding site. It is accompanied by Fe(2+) oxidation by Cu(2+)D6. Fe(3+) is then transferred from the binding site to the holding site. Cu(+)D6 is then re-oxidized by a Cu(2+) of the trinuclear cluster in about 200ms. The second Fe(2+) uptake and oxidation involve domain 4 and are under the kinetic control of a 200s change in the protein conformation. With transferrin and in the formed ceruloplasmin-transferrin adduct, two Fe(3+) are transferred from their holding sites to two C-lobes of two transferrins. The first transfer (~100s) is followed by conformation changes (500s) leading to the release of monoferric transferrin. The second transfer occurs in two steps in the 1000-10,000second range.Fe(3+) is transferred after Fe(2+) uptake and oxidation by ceruloplasmin to the C-lobe of transferrin in a protein-protein adduct. This adduct is in a permanent state of equilibrium with all the metal-free or bounded ceruloplasmin and transferrin species present in the medium.Ceruloplasmin is a go-between dietary or recycled Fe(2+) and transferrin transported Fe(3+)." @default.
- W2143662073 created "2016-06-24" @default.
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- W2143662073 date "2014-06-01" @default.
- W2143662073 modified "2023-10-18" @default.
- W2143662073 title "Iron uptake and transfer from ceruloplasmin to transferrin" @default.
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- W2143662073 doi "https://doi.org/10.1016/j.bbagen.2014.01.011" @default.
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