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Cited by 140Bacterial Genetics and BiotechnologyIron Metabolism and DisordersMetalloenzymes and iron-sulfur proteins

Bacterial iron detoxification at the molecular level

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Bradley, Justin M., Svistunenko, Dimitry A., Wilson, Michael T., Hemmings, Andrew M., Moore, Geoffrey R., Le Brun, Nick E.·2020·Journal of Biological Chemistry
DOI 10.1074/jbc.rev120.007746PMC PMC7762939
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Abstract

Iron is an essential micronutrient, and, in the case of bacteria, its availability is commonly a growth-limiting factor. However, correct functioning of cells requires that the labile pool of chelatable "free" iron be tightly regulated. Correct metalation of proteins requiring iron as a cofactor demands that such a readily accessible source of iron exist, but overaccumulation results in an oxidative burden that, if unchecked, would lead to cell death. The toxicity of iron stems from its potential to catalyze formation of reactive oxygen species that, in addition to causing damage to biological molecules, can also lead to the formation of reactive nitrogen species. To avoid iron-mediated oxidative stress, bacteria utilize iron-dependent global regulators to sense the iron status of the cell and regulate the expression of proteins involved in the acquisition, storage, and efflux of iron accordingly. Here, we survey the current understanding of the structure and mechanism of the important members of each of these classes of protein. Diversity in the details of iron homeostasis mechanisms reflect the differing nutritional stresses resulting from the wide variety of ecological niches that bacteria inhabit. However, in this review, we seek to highlight the similarities of iron homeostasis between different bacteria, while acknowledging important variations. In this way, we hope to illustrate how bacteria have evolved common approaches to overcome the dual problems of the insolubility and potential toxicity of iron.

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  • The majority of this iron is bound to enzymes, including those using FeS clusters or heme as cofactors.

    “The majority of this iron is bound to enzymes, including those using FeS clusters or heme as cofactors.125”

    From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [125]

    The Abstract (page unavailable) describes iron as a cofactor in many enzymes and identifies iron–sulfur clusters and heme as iron-containing cofactors. It does not say that the majority of cellular iron is bound to those enzymes; its statement that up to 25% of the proteome binds iron is a different measure. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

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Cited by

Sorted by citations

Authors
Bradley, J. M., Svistunenko, D. A., Wilson, M. T., Hemmings, A. M., Moore, G. R., & Le Brun, N. E.
Affiliations
  • University of East Anglia (GB)
  • University of Essex (GB)
Corresponding author
Bradley, Justin M.
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2020-12
Volume
295
Issue
51
Pages
17602-17623
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.rev120.007746
PMC
PMC7762939
OpenAlex
W3092359591
Cited by
140
References
18
Citations by year
2026: 20 · 2025: 34 · 2024: 29 · 2023: 22 · 2022: 20 · 2021: 15
FWCI
2.05
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, other-oa)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Open Access at Essex (University of Essex) (acceptedVersion)
  • UEA Digital Repository (University of East Anglia) (submittedVersion)
Funders
  • University of Essex
  • University of East Anglia
  • Directorate for Biological Sciences
  • Biotechnology and Biological Sciences Research Council (BB/R003203/1, BB/R002363/1)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Keywords
iron detoxification, iron acquisition, iron storage, iron efflux, oxidative stress, reactive oxygen species, reactive nitrogen species, iron toxicity
MeSH terms
Bacteria, Bacterial Proteins, Ferritins, Iron, Repressor Proteins, Siderophores, Reactive Oxygen Species, Oxidative Stress, Reactive Nitrogen Species

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