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 reductases in prokaryotes and eukaryotes.

Rita Mukhopadhyay1, Barry P Rosen

  • 1Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, 540 East Canfield Avenue, Detroit, MI 48201, USA. rmukhopad@med.wayne.edu

Environmental Health Perspectives
|November 12, 2002
PubMed
Summary

Environmental arsenic exposure drives the evolution of arsenate reductase enzymes. Both bacterial (E. coli ArsC) and eukaryotic (yeast Acr2p) enzymes detoxify arsenic, utilizing similar biochemical pathways and suggesting a common evolutionary origin.

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

Divergent evolutionary trajectories and mechanistic insights into arsenite and antimonite adaptation in the bacterium Achromobacter sp. As-55.

Ecotoxicology and environmental safety·2026
Same author

A Boronic Acid-Based Glutamine Analog Forms a Covalent Adduct with Kidney-Type Glutaminase and Suppresses Triple-Negative Breast Cancer Cell Proliferation.

Biomedicines·2026
Same author

Synergistic function of ars genes in arsenic detoxification and biosynthesis of organoarsenicals.

Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine·2026
Same author

Evolutionary Advantages of Multiple Arsenic Binding Sites in an ArsR Transcriptional Repressor.

Environmental science & technology·2025
Same author

Association of As(III) Methyltransferases and Radical S-Adenosylmethionine Enzymes.

Environmental science & technology·2025
Same author

The Thioredoxin System Powers ArsM-Mediated Arsenite Methylation in <i>Hymenobacter edaphi</i>.

Environmental science & technology·2025

Area of Science:

  • Biochemistry
  • Enzymology
  • Evolutionary Biology

Background:

  • Arsenic is widespread in the environment, necessitating detoxification mechanisms.
  • Arsenate reductase enzymes catalyze the critical reduction of arsenate [As(V)] to arsenite [As(III)].
  • At least three enzyme families have evolved independently for arsenate reduction.

Purpose of the Study:

  • To characterize two distinct arsenate reductase enzymes: prokaryotic ArsC from E. coli and eukaryotic Acr2p from S. cerevisiae.
  • To investigate the evolutionary relationships and biochemical mechanisms of these enzymes.

Main Methods:

  • Biochemical assays to determine enzyme properties and reducing equivalents.
  • X-ray crystallography to solve the structure of the bacterial ArsC enzyme.

Related Experiment Videos

  • Sequence analysis to compare active site motifs.

    • Main Results:

    • Both E. coli ArsC and yeast Acr2p utilize glutaredoxin and reduced glutathione for reducing equivalents.
    • The crystal structure of ArsC revealed covalent enzyme-arsenic intermediates, confirming its catalytic mechanism.
    • A conserved active site motif HC(X)(5)R in Acr2p is shared with protein phosphotyrosine phosphatases and rhodanases.

    Conclusions:

    • Despite lacking sequence homology, bacterial and eukaryotic arsenate reductases share functional similarities.
    • The conserved active site motif suggests a potential evolutionary link to other enzyme families.
    • These findings support the hypothesis that arsenate reductases evolved from an ancestral oxyanion-binding protein via convergent evolution.