Evidence map›Paper›PMID 32279136›Full record

ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2020

Functional mononuclear molybdenum enzymes: challenges and triumphs in molecular cloning, expression, and isolation.

Breeanna Mintmier, Samih Nassif, John F Stolz, Partha Basu

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Review
  2. Enhanced Bioremediation Potential ofFrontiers in microbiology · 2022
    Article
  3. Kinetic consequences of the endogenous ligand to molybdenum in the DMSO reductase family: a case study with periplasmic nitrate reductase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021
    Article
  4. 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.

Breeanna MintmierDepartment of Chemistry and Chemical Biology, Indiana University-Purdue University Indianapolis, 402 N Blackford St, Indianapolis, IN, 46202, USA.
Samih NassifDepartment of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA, USA.
John F StolzDepartment of Biological Sciences, Duquesne University, Pittsburgh, PA, USA.
Partha BasuDepartment of Chemistry and Chemical Biology, Indiana University-Purdue University Indianapolis, 402 N Blackford St, Indianapolis, IN, 46202, USA. basup@iupui.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mononuclear molybdenum enzymes catalyze a variety of reactions that are essential in the cycling of nitrogen, carbon, arsenic, and sulfur. For decades, the structure and function of these crucial enzymes have been investigated to develop a fundamental knowledge for this vast family of enzymes and the chemistries they carry out. Therefore, obtaining abundant quantities of active enzyme is necessary for exploring this family's biochemical capability. This mini-review summarizes the methods for overexpressing mononuclear molybdenum enzymes in the context of the challenges encountered in the process. Effective methods for molybdenum cofactor synthesis and incorporation, optimization of expression conditions, improving isolation of active vs. inactive enzyme, incorporation of additional prosthetic groups, and inclusion of redox enzyme maturation protein chaperones are discussed in relation to the current molybdenum enzyme literature. This article summarizes the heterologous and homologous expression studies providing underlying patterns and potential future directions.

Indexed as

Cloning, MolecularIron-Sulfur ProteinsMetalloproteinsMolecular StructureMolybdenumOxidoreductasesSulfite OxidaseXanthine Oxidasedimethyl sulfoxide reductaseIron-Sulfur ProteinsMetalloproteinsMolybdenumOxidoreductasesSulfite OxidaseXanthine OxidaseDimethyl sulfoxide reductase familyMolybdenumPterinSulfite oxidase familyXanthine oxidase family

Identifiers

PMID32279136

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.