Evidence map›Paper›PMID 22661719›Full record

ArticleThe Journal of biological chemistry2012

A low pKa cysteine at the active site of mouse methionine sulfoxide reductase A.

Jung Chae Lim, James M Gruschus, Geumsoo Kim, Barbara S Berlett, Nico Tjandra, Rodney L Levine

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Improving pJournal of chemical theory and computation · 2025
    Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Detection of electrophile-sensitive proteins.Biochimica et biophysica acta · 2014
    Review
  14. Review
  15. Methionine oxidation and reduction in proteins.Biochimica et biophysica acta · 2014
    Review
  16. Article
  17. Protein Oxidative Modifications: Beneficial Roles in Disease and Health.Journal of biochemical and pharmacological research · 2013
    Article
  18. The role of methionine sulfoxide reductase in redox signaling.The Journal of biological chemistry · 2012
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Jung Chae LimLaboratory of Biochemistry, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-8012, USA.
James M Gruschus
Geumsoo Kim
Barbara S Berlett
Nico Tjandra
Rodney L Levine
National Institutes of Health · US

Funding

Oxidative Modification Of ProteinsZIAHL000225 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI LEVINE, RODNEY L. · 2009 to 2025
$35.2M
Nmr Studies Of The Regulation Of Cell SignalingZIAHL001048 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI TJANDRA, NICO · 2009 to 2025
$20.1M
Intramural NIH HHS
6 · The paper itself

Abstract

Methionine sulfoxide reductase A is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide. Recently it has also been shown to catalyze the reverse reaction, oxidizing methionine residues to methionine sulfoxide. A cysteine at the active site of the enzyme is essential for both reductase and oxidase activities. This cysteine has been reported to have a pK(a) of 9.5 in the absence of substrate, decreasing to 5.7 upon binding of substrate. Using three independent methods, we show that the pK(a) of the active site cysteine of mouse methionine sulfoxide reductase is 7.2 even in the absence of substrate. The primary mechanism by which the pK(a) is lowered is hydrogen bonding of the active site Cys-72 to protonated Glu-115. The low pK(a) renders the active site cysteine susceptible to oxidation to sulfenic acid by micromolar concentrations of hydrogen peroxide. This characteristic supports a role for methionine sulfoxide reductase in redox signaling.

Indexed as

AnimalsCatalysisCatalytic DomainCysteineHydrogen BondingMethionineMethionine Sulfoxide ReductasesMiceOxidation-ReductionCysteineMethioninemethionine sulfoxide reductaseMethionine Sulfoxide Reductases

Identifiers

PMID22661719
PMCPMC3408155
OpenAlexW2080584906

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.