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The biological inorganic chemistry of zinc ions

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Krężel, Artur, Maret, Wolfgang·2016·Archives of Biochemistry and Biophysics
DOI 10.1016/j.abb.2016.04.010PMC PMC5120989
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Abstract

The solution and complexation chemistry of zinc ions is the basis for zinc biology. In living organisms, zinc is redox-inert and has only one valence state: Zn(II). Its coordination environment in proteins is limited by oxygen, nitrogen, and sulfur donors from the side chains of a few amino acids. In an estimated 10% of all human proteins, zinc has a catalytic or structural function and remains bound during the lifetime of the protein. However, in other proteins zinc ions bind reversibly with dissociation and association rates commensurate with the requirements in regulation, transport, transfer, sensing, signalling, and storage. In contrast to the extensive knowledge about zinc proteins, the coordination chemistry of the “mobile” zinc ions in these processes, i.e. when not bound to proteins, is virtually unexplored and the mechanisms of ligand exchange are poorly understood. Knowledge of the biological inorganic chemistry of zinc ions is essential for understanding its cellular biology and for designing complexes that deliver zinc to proteins and chelating agents that remove zinc from proteins, for detecting zinc ion species by qualitative and quantitative analysis, and for proper planning and execution of experiments involving zinc ions and nanoparticles such as zinc oxide (ZnO). In most investigations, reference is made to zinc or Zn2+ without full appreciation of how biological zinc ions are buffered and how the d-block cation Zn2+ differs from s-block cations such as Ca2+ with regard to significantly higher affinity for ligands, preference for the donor atoms of ligands, and coordination dynamics. Zinc needs to be tightly controlled. The interaction with low molecular weight ligands such as water and inorganic and organic anions is highly relevant to its biology but in contrast to its coordination in proteins has not been discussed in the biochemical literature. From the discussion in this article, it is becoming evident that zinc ion speciation is important in zinc biochemistry and for biological recognition as a variety of low molecular weight zinc complexes have already been implicated in biological processes, e.g. with ATP, glutathione, citrate, ethylenediaminedisuccinic acid, nicotianamine, or bacillithiol.

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  • Addition of ZnCl2 in the fluids decreases the pH from 8.6 to 6.7 (measured at 25 °C), caused by the formation of Zn(II) aquo complexes.

    “Addition of ZnCl2 in the fluids decreases the pH from 8.6 to 6.7 (measured at 25 °C), caused by the formation of Zn(II) aquo complexes41.”

    From Acceleration of dolomitization by zinc in saline waters (2019) · cites this paper as [41]

    The “Zinc(II) aquo complexes and hydroxides” section (page not provided) explains that zinc aquo complexes release protons and that ZnCl2 solutions can be acidic. It does not report adding ZnCl2 to the specified fluids, a pH change from 8.6 to 6.7, or that measurement at 25 °C. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • For Zn2+ and Cu+, the notional free metal pool is less than one atom per cell at equilibrium, and metal mobility relies on ligand exchange chemistry.

    “For Zn2+ and Cu+, however, the notional free metal pool is less than one atom per cell at equilibrium, and the mobility of metals relies on ligand exchange chemistry.3,31,32”

    From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [32]

    The Conclusions (page unavailable) say that ligand-exchange kinetics enable zinc redistribution, and the zinc-speciation section says zinc transport involves multiple ligand exchanges. The paper does not establish a free pool of less than one atom per cell at equilibrium or extend these statements to Cu+; its discussion of the cellular free pool instead estimates zinc concentrations at a few hundred picomolar. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • Zinc forms strong complexes with water and several anions, and has a flexible coordination between 4, 5 and 6, which makes it an efficient catalyst in biological context.

    “Zinc forms strong complexes with water and several anions, and has a flexible coordination between 4, 5 and 6, which makes it an efficient catalyst in biological context41.”

    From Acceleration of dolomitization by zinc in saline waters (2019) · cites this paper as [41]

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Authors
Krężel, A., & Maret, W.
Affiliations
  • University of Wrocław (PL)
  • King's College London (GB)
Corresponding author
Maret, Wolfgang
ORCID
Venue
Archives of Biochemistry and Biophysics
Publisher
Elsevier BV
Published
2016-12
Volume
611
Pages
3-19
ISSN
0003-9861 (ISSN-L)
DOI
10.1016/j.abb.2016.04.010
PMC
PMC5120989
OpenAlex
W2344658806
Cited by
768
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0
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FWCI
53.39
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journal article
Language
en
Open access
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  • Archives of Biochemistry and Biophysics (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Research Portal (King's College London) (submittedVersion, cc-by)
Funders
  • National Science Centre and the Polish Ministry of Science and Higher Education (2012/07/E/NZ1/01894)
  • Iuventus Plus (IP2012 018272)
  • Biotechnology and Biological Sciences Research Council (BB/K001442/1)
Topics
  • Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
  • Health Sciences › Medicine › Oncology › Metal complexes synthesis and properties
  • Physical Sciences › Chemistry › Organic Chemistry › Inorganic and Organometallic Chemistry
Keywords
zinc ions, zinc coordination chemistry, ligand exchange, zinc ion detection, zinc oxide nanoparticles, zinc transport
MeSH terms
Anions, Buffers, Catalysis, Cations, Chelating Agents, Humans, Hydrogen-Ion Concentration, Ligands, Oxidation-Reduction, Proteins, Solubility, Temperature, Zinc, Chemistry, Bioinorganic, Signal Transduction

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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