Evidence map›Paper›PMID 32022353›Full record

ReviewProtein science : a publication of the Protein Society2020

Structure, function, and biosynthesis of nickel-dependent enzymes.

Marila Alfano, Christine Cavazza

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

65 citing papers in PubMed, 171 citations in OpenAlex.

  1. Article
  2. Article
  3. Nickel Toxicity in Plants.International journal of molecular sciences · 2026
    Review
  4. Article
  5. Article
  6. Nickel Single-Atom Nanozyme for Multimodal Cancer Therapy.ACS applied materials & interfaces · 2026
    Article
  7. Cobalt mitigates zinc-starvation effects in Pseudomonas aeruginosa.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Article
  8. From single step hops to emergent biological phenomena.Journal of inorganic biochemistry · 2026
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Microorganisms · 2025
    Article
  16. Article
  17. Identification of glyoxalase A in group BInfection and immunity · 2025
    Article
  18. Article
  19. Insights into the Role of the D-Cluster in [NiFe]-CODH from Rhodospirillum Rubrum.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  20. Article

5 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Marila AlfanoUniversity of Grenoble Alpes, CEA, CNRS, IRIG, CBM, Grenoble, France.ORCID 0000-0002-8460-0227
Christine CavazzaUniversity of Grenoble Alpes, CEA, CNRS, IRIG, CBM, Grenoble, France.ORCID 0000-0002-3657-1302
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nickel enzymes, present in archaea, bacteria, plants, and primitive eukaryotes are divided into redox and nonredox enzymes and play key functions in diverse metabolic processes, such as energy metabolism and virulence. They catalyze various reactions by using active sites of diverse complexities, such as mononuclear nickel in Ni-superoxide dismutase, glyoxylase I and acireductone dioxygenase, dinuclear nickel in urease, heteronuclear metalloclusters in [NiFe]-carbon monoxide dehydrogenase, acetyl-CoA decarbonylase/synthase and [NiFe]-hydrogenase, and even more complex cofactors in methyl-CoM reductase and lactate racemase. The presence of metalloenzymes in a cell necessitates a tight regulation of metal homeostasis, in order to maintain the appropriate intracellular concentration of nickel while avoiding its toxicity. As well, the biosynthesis and insertion of nickel active sites often require specific and elaborated maturation pathways, allowing the correct metal to be delivered and incorporated into the target enzyme. In this review, the phylogenetic distribution of nickel enzymes will be briefly described. Their tridimensional structures as well as the complexity of their active sites will be discussed. In view of the latest findings on these enzymes, a special focus will be put on the biosynthesis of their active sites and nickel activation of apo-enzymes.

Indexed as

BiocatalysisCatalytic DomainDioxygenasesEnzymesHydrogenaseLactoylglutathione LyaseNickelProtein ConformationSuperoxide DismutaseUreaseaci-reductone oxidase (CO-forming)DioxygenasesEnzymesHydrogenaseLactoylglutathione LyaseNickelnickel-iron hydrogenaseSuperoxide DismutaseUreaseenzyme maturationmetalloclustermetalloenzymesnickel active siteredox enzymes

Identifiers

PMID32022353
PMCPMC7184782
OpenAlexW3005140868

What OpenQuestion holds

Textmetadata
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.