Evidence map›Paper›PMID 30735836›Full record

ReviewFree radical biology & medicine2019

Evolutionary adaptations that enable enzymes to tolerate oxidative stress.

James A Imlay, Ramakrishnan Sethu, Sanjay Kumar Rohaun

Open access · greenAbstract readReview
In one paragraph

Review in Free radical biology & medicine, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.5field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 49 citations in OpenAlex.

  1. Electroenzymatic COAngewandte Chemie (International ed. in English) · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. New-to-nature CONature communications · 2024
    Article
  7. Elucidating the Role of OACS environmental Au · 2024
    Article
  8. Review
  9. Article
  10. Frontiers in microbiology · 2024
    Article
  11. The Fe and Zn cofactor dilemma.Biochimica et biophysica acta. Proteins and proteomics · 2023
    Review
  12. Article
  13. A mineral-based origin of Earth's initial hydrogen peroxide and molecular oxygen.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. The ArcAB Two-Component System: Function in Metabolism, Redox Control, and Infection.Microbiology and molecular biology reviews : MMBR · 2022
    Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. How Microbes Evolved to Tolerate Oxygen.Trends in microbiology · 2021
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

James A ImlayDepartment of Microbiology, University of Illinois, 601 S. Goodwin Ave, Urbana, IL, 61801, USA. Electronic address: jimlay@illinois.edu.
Ramakrishnan SethuDepartment of Microbiology, University of Illinois, 601 S. Goodwin Ave, Urbana, IL, 61801, USA.
Sanjay Kumar RohaunDepartment of Microbiology, University of Illinois, 601 S. Goodwin Ave, Urbana, IL, 61801, USA.
University of Illinois Urbana-Champaign · USGoodwin College · US

Funding

The Physiology of Oxidative Stress in Escherichia coliR01GM049640 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI IMLAY, JAMES A. · 1994 to 2024
$6.9M
The Physiology of Oxidative Stress in Escherichia coliR37GM049640 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI IMLAY, JAMES A. · 2007 to 2016
$5.3M
Soft Metal, Disulfide, and Cysteine Stresses in Escherichia coliR01GM101012 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI IMLAY, JAMES A. · 2012 to 2020
$2.2M
NIGMS NIH HHS R01 GM049640NIGMS NIH HHS R01 GM101012NIGMS NIH HHS R37 GM049640
6 · The paper itself

Abstract

Biochemical mechanisms emerged and were integrated into the metabolic plan of cellular life long before molecular oxygen accumulated in the biosphere. When oxygen levels finaly rose, they threatened specific types of enzymes: those that use organic radicals as catalysts, and those that depend upon iron centers. Nature has found ways to ensure that such enzymes are still used by contemporary organisms. In some cases they are restricted to microbes that reside in anoxic habitats, but in others they manage to function inside aerobic cells. In the latter case, it is frequently true that the ancestral enzyme has been modified to fend off poisoning. In this review we survey a range of protein adaptations that permit radical-based and low-potential iron chemistry to succeed in oxic environments. In many cases, accessory domains shield the vulnerable radical or metal center from oxygen. In others, the structures of iron cofactors evolved to less oxidizable forms, or alternative metals replaced iron altogether. The overarching view is that some classes of biochemical mechanism are intrinsically incompatible with the presence of oxygen. The structural modification of target enzymes is an under-recognized response to this problem.

Indexed as

Adaptation, PhysiologicalOxidative StressCatalysisFree RadicalsIronOxidation-ReductionOxygenFree RadicalsIronOxygenHydrogen peroxideIron-sulfur clustersObligate anaerobiosisRadical enzymesSuperoxide

Identifiers

PMID30735836
PMCPMC6684875
OpenAlexW2914190449

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.