Zinc trafficking: 1,10-phenanthroline, glutathione, and other metal binding ligands form adducts with proteomic Zn2+ (2023)

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Volume 15 Issue 5 May 2023 (In Progress)
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Kaniz Fatema,

Kaniz Fatema

Department of Chemistry, Marquette University

,

Milwaukee, WI 53201-1881

,

USA

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Eric Lund,

Eric Lund

Abbott Laboratories

,

Abbott Park, IL 60064, USA

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 David H Petering

David H Petering

Department of Chemistry and Biochemistry, University of Wisconsin-Milwaukee

,

Milwaukee, WI 53201

,

USA

Correspondence: Department of Chemistry and Biochemistry, University of Wisconsin-Milwaukee, Milwaukee, WI 53201, USA. Tel: +414-229-5853; E-mail: petering@uwm.edu

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Published:

21 April 2023

Article history

Received:

01 December 2022

Accepted:

13 March 2023

Published:

21 April 2023

Corrected and typeset:

10 May 2023

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    Kaniz Fatema and others, Zinc trafficking: 1,10-phenanthroline, glutathione, and other metal binding ligands form adducts with proteomic Zn2+, Metallomics, Volume 15, Issue 5, May 2023, mfad026, https://doi.org/10.1093/mtomcs/mfad026

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Abstract

Hypotheses were tested that the proteome of pig kidney LLC-PK1 cells (i) contains Zn-proteins that react with a diversity of native and pharmacologically active metal-binding ligands to form ternary complexes and (ii) includes proteins that bind Zn2+ nonspecifically and together form ternary adducts with a variety of metal-binding agents. The method to observe ternary complex formation with Zn-proteins and proteome•Zn involved preformation of fluorescent TSQ [6-Methoxy-(8-p-toluenesulfonamido)quinoline]–Zn-proteins and/or proteome•Zn–TSQ adducts followed by competitive reaction with selected ligands. The loss of TSQ-dependent fluorescence signaled the replacement of TSQ by the competing ligand in the starting adducts. In vitro, 1,10-phenanthroline competed effectively with TSQ for binding to Zn-proteins in the proteome. The successful competition of 1,10-phenanthroline with TSQ–Zn-proteins was also observed in cells. Similarly, 1,10-phenanthroline was shown to bind to a sizable fraction of Zn2+ associated adventitiously with proteome (proteome•Zn). Other synthetic ligands that bind to Zn-proteins and proteome•Zn include 2,2-bipyridyl, 8-hydroxyquinoline, 2,2ʹ-dicarboxypyridine, and pyrithione. Such results suggest that ligand binding to such sites may play a role in the observed biological effects of these and other metal-binding molecules. Although cysteine does not significantly compete with TSQ, glutathione displaces TSQ from Zn-proteins and proteome•Zn at concentrations well below those found in cells, implying that ternary complex formation involving glutathione may be physiologically significant.

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Zinc trafficking: 1,10-phenanthroline, glutathione, and other metal binding ligands form adducts with proteomic Zn2+ (3)

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We have hypothesized that zinc-trafficking involves Zn2+ non-specifically bound to proteomic sites (proteome•Zn) that is mobilized to apo-Zn-proteins by glutathione (GSH) through an intermediate proteome•Zn-GS species. Utilizing TSQ fluorescent adducts with Zn-proteins and proteome•Zn, we demonstrated that GSH, 1,10-phenantroline, and other zinc-binding ligands form ternary complexes with Zn-proteins and proteome•Zn.

© The Author(s) 2023. Published by Oxford University Press.

This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

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