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The Cu(II) affinity constant and reactivity of Hepcidin-25, the main iron regulator in human blood

Płonka, Dawid and Wiśniewska, Marta and Ziemska-Legiecka, Joanna and Grynberg, Marcin and Bal, Wojciech (2023) The Cu(II) affinity constant and reactivity of Hepcidin-25, the main iron regulator in human blood. Journal of inorganic biochemistry, 248 . p. 112364. ISSN 1873-3344

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Official URL: https://www.sciencedirect.com/science/article/pii/...

Abstract

Hepcidin is an iron regulatory hormone that does not bind iron directly. Instead, its mature 25-peptide form (H25) contains a binding site for other metals, the so-called ATCUN/NTS (amino-terminal Cu/Ni binding site). The Cu(II)-hepcidin complex was previously studied, but due to poor solubility and difficult handling of the peptide the definitive account on the binding equilibrium was not obtained reliably. In this study we performed a series of fluorescence competition experiments between H25 and its model peptides containing the same ATCUN/NTS site and determined the Cu(II) conditional binding constant of the CuH25 complex at pH 7.4, CK7.4 = 4 ± 2 × 1014 M−1. This complex was found to be very inert in exchange reactions and poorly reactive in the ascorbate consumption test. The consequences of these findings for the putative role of Cu(II) interactions with H25 are discussed.

Item Type:Article
Uncontrolled Keywords:Hepcidin Copper complex ATCUN Binding constant Redox Kinetics
Subjects:Q Science > QD Chemistry
Q Science > QP Physiology
Divisions:Department of Biophysics
ID Code:2322
Deposited By: Mr Dawid Płonka
Deposited On:14 Sep 2023 06:58
Last Modified:21 May 2024 11:26

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