Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Arsenate reduction: thiol cascade chemistry with convergent evolution.

Joris Messens1, Simon Silver

  • 1Brussels Center for Redox Biology, Department of Molecular and Cellular Interactions, Vlaams interuniversitair Instituut voor Biotechnologie (VIB) at the Vrije Universiteit Brussel (VUB), Pleinlaan 2, 1050 Brussel, Belgium. joris.messens@vub.ac.be

Journal of Molecular Biology
|August 15, 2006
PubMed
Summary

Arsenate reductases (ArsC) are diverse enzymes crucial for arsenic detoxification. They reduce toxic arsenate to less harmful arsenite through various mechanisms, aiding microbial and cellular resistance.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Hetero-oligomerization drives structural plasticity of eukaryotic peroxiredoxins.

Nature chemical biology·2026
Same author

Peroxidasin enables melanoma immune escape by inhibiting natural killer cell cytotoxicity.

Molecular oncology·2026
Same author

Pervanadate-induced oxidation relieves autoinhibition of the protein tyrosine kinase SRC.

Science signaling·2026
Same author

Single-cell imaging of liver metabolic dynamics using fluorescent biosensors.

Trends in endocrinology and metabolism: TEM·2025
Same author

A color-tailored fluorogenic sensor for hydrogen peroxide.

Nature chemical biology·2025
Same author

Metabolic dysfunction-associated steatohepatitis reduces hepatic H<sub>2</sub>S-producing enzymes altering persulfidome composition.

Redox biology·2025

Area of Science:

  • Biochemistry
  • Environmental Science
  • Microbiology

Background:

  • Arsenic's environmental prevalence drives the evolution of arsenate-reducing enzymes.
  • Arsenate reductases (ArsC) exhibit diverse sequences, structures, and catalytic mechanisms.
  • These enzymes are classified based on structure, reduction pathways, and catalytic cysteine location.

Purpose of the Study:

  • To review and categorize the different classes of arsenate reductases.
  • To elucidate the distinct reduction mechanisms employed by various arsenate reductases.
  • To highlight the role of these enzymes in arsenic resistance across different organisms.

Main Methods:

  • Comparative analysis of arsenate reductase sequences and structures.
  • Classification of enzymes based on their reduction mechanisms and cofactor dependencies.

Related Experiment Videos

  • Review of literature on enzyme function and cellular localization.
  • Main Results:

    • ArsC enzymes are divided into thioredoxin-linked and glutaredoxin-linked classes.
    • The ArrAB complex represents a distinct bacterial arsenate reductase system.
    • Arsenic(III) methylase exhibits arsenate reductase activity linked to methylation.

    Conclusions:

    • Arsenate reductases are vital for arsenic detoxification and resistance.
    • Enzyme diversity reflects adaptation to environmental arsenic.
    • Understanding these enzymes is key to addressing arsenic toxicity.