Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidation.

The Biochemical journal - 15 Feb 2016

Poynton Rebecca A, Peskin Alexander V, Haynes Alexina C, Lowther W Todd, Hampton Mark B, Winterbourn Christine C

Abstract excerpt

Mammalian 2-cysteine peroxiredoxins (Prxs) are susceptible to hyperoxidation by excess H2O2. The cytoplasmic family member Prx2 hyperoxidizes more readily than mitochondrial Prx3 due to slower dimerization of the sulfenic acid (SpOH) intermediate. Four variant amino acids near the C-terminus have been shown to contribute to this difference. We have performed kinetic analysis of the relationship between...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to HeLa Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kinetics

Share to Oxidation-Reduction

Share to Peroxiredoxins

Share to Protein Conformation

Share to Recombinant Proteins

Share to Sequence Homology, Amino Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 26614766
DOI: 10.1042/BJ20150572
PMCID: PMC4859152

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidation.PMID 26614766Read ↗

Molecular basis for the resistance of human mitochondrial 2-Cys peroxiredoxin 3 to hyperoxidation.Semantic proximity Read ↗

Quaternary structure influences the peroxidase activity of peroxiredoxin 3.Semantic proximity Read ↗

In vivo parameters influencing 2-Cys Prx oligomerization: The role of enzyme sulfinylation.Semantic proximity Read ↗

Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2.Semantic proximity Read ↗

Oxidant-induced Interprotein Disulfide Formation in Cardiac Protein DJ-1 Occurs via an Interaction with Peroxiredoxin 2.Semantic proximity Read ↗

PRDX4, an endoplasmic reticulum-localized peroxiredoxin at the crossroads between enzymatic oxidative protein folding and nonenzymatic protein oxidation.Semantic proximity Read ↗

Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4.Semantic proximity Read ↗

Glutathionylation of peroxiredoxin I induces decamer to dimers dissociation with concomitant loss of chaperone activity.Semantic proximity Read ↗

Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin.Semantic proximity Read ↗

Microbial 2-Cys Peroxiredoxins: Insights into Their Complex Physiological Roles.Semantic proximity Read ↗

Crystal structure of reduced and of oxidized peroxiredoxin IV enzyme reveals a stable oxidized decamer and a non-disulfide-bonded intermediate in the catalytic cycle.Semantic proximity Read ↗

Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.