Evidence map›Paper›PMID 31277490›Full record

ReviewMolecules (Basel, Switzerland)2019

Formation of Unstable and very Reactive Chemical Species Catalyzed by Metalloenzymes: A Mechanistic Overview.

Henrique S Fernandes, Carla S Silva Teixeira, Sérgio F Sousa, Nuno M F S A Cerqueira

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

9 citing papers in PubMed, 19 citations in OpenAlex.

  1. All-in-One COAccounts of chemical research · 2024
    Review
  2. Classifying metal-binding sites with neural networks.Protein science : a publication of the Protein Society · 2023
    Article
  3. Phosphorus containing analogues of SAHA as inhibitors of HDACs.Journal of enzyme inhibition and medicinal chemistry · 2022
    Article
  4. Article
  5. Article
  6. Protein metalation in biology.Current opinion in chemical biology · 2022
    Review
  7. Immunological Mechanisms of Metal Allergies and the Nickel-Specific TCR-pMHC Interface.International journal of environmental research and public health · 2021
    Review
  8. Metal-ion promiscuity of microbial enzyme DapE at its second metal-binding site.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021
    Article
  9. 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

4 authors at 1 institution in 1 country.

Henrique S FernandesUCIBIO@REQUIMTE, BioSIM, Departamento de Biomedicina, Faculdade de Medicina da Universidade do Porto, Alameda Professor Hernâni Monteiro, 4200-319 Porto, Portugal.ORCID 0000-0002-9280-1838
Carla S Silva TeixeiraUCIBIO@REQUIMTE, BioSIM, Departamento de Biomedicina, Faculdade de Medicina da Universidade do Porto, Alameda Professor Hernâni Monteiro, 4200-319 Porto, Portugal.ORCID 0000-0002-8422-9392
Sérgio F SousaUCIBIO@REQUIMTE, BioSIM, Departamento de Biomedicina, Faculdade de Medicina da Universidade do Porto, Alameda Professor Hernâni Monteiro, 4200-319 Porto, Portugal.ORCID 0000-0002-6560-5284
Nuno M F S A CerqueiraUCIBIO@REQUIMTE, BioSIM, Departamento de Biomedicina, Faculdade de Medicina da Universidade do Porto, Alameda Professor Hernâni Monteiro, 4200-319 Porto, Portugal. nunoscerqueira@med.up.pt.
Universidade do Porto · PT

Funding

Fundação para a Ciência e a Tecnologia SFRH/BD/115396/2016, SFRH/BD/114886/2016, UID/Multi/04378/2019, IF/00052/2014, IF/01310/2013
6 · The paper itself

Abstract

Nature has tailored a wide range of metalloenzymes that play a vast array of functions in all living organisms and from which their survival and evolution depends on. These enzymes catalyze some of the most important biological processes in nature, such as photosynthesis, respiration, water oxidation, molecular oxygen reduction, and nitrogen fixation. They are also among the most proficient catalysts in terms of their activity, selectivity, and ability to operate at mild conditions of temperature, pH, and pressure. In the absence of these enzymes, these reactions would proceed very slowly, if at all, suggesting that these enzymes made the way for the emergence of life as we know today. In this review, the structure and catalytic mechanism of a selection of diverse metalloenzymes that are involved in the production of highly reactive and unstable species, such as hydroxide anions, hydrides, radical species, and superoxide molecules are analyzed. The formation of such reaction intermediates is very difficult to occur under biological conditions and only a rationalized selection of a particular metal ion, coordinated to a very specific group of ligands, and immersed in specific proteins allows these reactions to proceed. Interestingly, different metal coordination spheres can be used to produce the same reactive and unstable species, although through a different chemistry. A selection of hand-picked examples of different metalloenzymes illustrating this diversity is provided and the participation of different metal ions in similar reactions (but involving different mechanism) is discussed.

Indexed as

CatalysisEnzymesHydroxidesMetalloproteinsSuperoxidesEnzymeshydroxide ionHydroxidesMetalloproteinsSuperoxidescatalytic mechanismironmetalloenzymesmolybdenumtransition metalszinc

Identifiers

PMID31277490
PMCPMC6651669
OpenAlexW2954163989

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.