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Literature summary for 1.16.3.1 extracted from

  • Cortes, L.; Roberts, B.R.; Wedd, A.G.; Xiao, Z.
    Molecular aspects of a robust assay for ferroxidase function of ceruloplasmin (2017), Inorg. Chem., 56, 5275-5284 .
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ a multicopper oxidase Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4 Fe(II) + 4 H+ + O2 Homo sapiens
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4 Fe(III) + 2 H2O
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4 Fe(II) + 4 H+ + O2
-
Homo sapiens 4 Fe(III) + 2 H2O
-
?
additional information development of the classic chromophoric complex FeIIHx(Tar)2 (H2Tar), 4-(2-thiazolylazo)-resorcinol (x = 0-2) as a robust substrate for evaluation of the ferroxidase function of ceruloplasmin and related enzymes. The catalysis can be followed conveniently in real-time by monitoring the solution absorbance at 720 nm, a fingerprint of FeIIHx(Tar)2. The complex is oxidized to its ferric form FeIIIHx(Tar)2. Fe(II) is transferred formally from FeIIHx(Tar)2 to the substrate docking/oxidation (SDO) site(s) in ceruloplasmin, followed by oxidation to product Fe(III) that is trapped again by the ligand. Each Tar ligand in the above bis-complex coordinates the metal center in a meridional tridentate mode involving a pH-sensitive -OH group (pKa >12), and this imposes rapid Fe(II) and Fe(III) transfer kinetics to facilitate the catalytic process. Method evaluation and proposed mechanism, detailed overview Homo sapiens ?
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?

Synonyms

Synonyms Comment Organism
ceruloplasmin
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Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Homo sapiens

General Information

General Information Comment Organism
physiological function ceruloplasmin is one of the most complex multicopper oxidase enzymes and plays an essential role in the metabolism of iron in mammals. Ferrous ion supplied by the ferroportin exporter is converted by ceruloplasmin to ferric ion that is accepted by plasma metallo-chaperone transferrin. The multicopper oxidase enzymes mediate transfer of the iron from the cell export pump ferroportin to the plasma metallo-chaperone transferrin. Specifically, they are responsible for conversion of Fe(II) to Fe(III), the form in which it is transported in the blood by transferrin Homo sapiens