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Cited by 3Glutathione Transferases and PolymorphismsArsenic contamination and mitigationRedox biology and oxidative stress

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Proposed mechanism for monomethylarsonate reductase activity of human omega-class glutathione transferase GSTO1-1

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Oakley, Aaron J.·2022·Biochemical and Biophysical Research Communications
DOI 10.1016/j.bbrc.2021.12.072

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Abstract

Contamination of drinking water with toxic inorganic arsenic is a major public health issue. The mechanisms of enzymes and transporters in arsenic elimination are therefore of interest. The human omega-class glutathione transferases have been previously shown to possess monomethylarsonate (V) reductase activity. To further understanding of this activity, molecular dynamics of human GSTO1-1 bound to glutathione with a monomethylarsonate isostere were simulated to reveal putative monomethylarsonate binding sites on the enzyme. The major binding site is in the active site, adjacent to the glutathione binding site. Based on this and previously reported biochemical data, a reaction mechanism for this enzyme is proposed. Further insights were gained from comparison of the human omega-class GSTs to homologs from a range of animals.

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Metadata

Authors
Oakley, A. J.
Affiliations
University of Wollongong (AU)
Corresponding author
Oakley, Aaron J.
ORCID
Oakley, Aaron J.
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2022-01
Volume
590
Pages
7-13
ISSN
0006-291X (ISSN-L)
DOI
10.1016/j.bbrc.2021.12.072
OpenAlex
W4225861523
Cited by
3
References
2
Citations by year
2025: 2 · 2022: 1
FWCI
0.08
Type
journal article
Language
en
Open access
Licence
Locations
  • Biochemical and Biophysical Research Communications (publishedVersion)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • Research Online (University of Wollongong) (submittedVersion)
  • Figshare (submittedVersion)
Funders
  • National Health and Medical Research Council (APP1124673, APP1156455)
  • National Institutes of Health (R01-GM129325)
  • National Institute of Allergy and Infectious Diseases
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
  • Physical Sciences › Environmental Science › Environmental Chemistry › Arsenic contamination and mitigation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords
arsenic detoxification, inorganic arsenic, glutathione binding site, enzyme mechanism, molecular dynamics simulation, active site
MeSH terms
Amino Acid Sequence, Glutathione Transferase, Humans, Models, Molecular, Oxidoreductases, Catalytic Domain

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