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

The significance of type II and PrxQ peroxiredoxins for antioxidative stress response in the purple bacterium Rhodobacter sphaeroides.

The Journal of biological chemistry - 21 Sept 2007

Wakita Masahiro, Masuda Shinji, Motohashi Ken, Hisabori Toru, Ohta Hiroyuki, Takamiya Ken-ichiro

Abstract excerpt

Two peroxiredoxins, classified as Type II and PrxQ, were characterized in the purple non-sulfur photosynthetic bacterium Rhodobacter sphaeroides. Both recombinant proteins showed remarkable thioredoxin-dependent peroxidase activity with broad substrate specificity in vitro. Nevertheless, PrxQ of R. sphaeroides, unlike typical PrxQs studied to date, does not contain one of the two conserved catalytic Cys residues....

Read the complete abstract on PubMed

Topics

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

Share to Cysteine
Share to Genome, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxidation-Reduction

Share to Oxygen

Share to Peroxidases

Share to Peroxiredoxins

Share to Rhodobacter sphaeroides

Share to Sulfhydryl Compounds

Source

Identifiers

PMID: 17644813
DOI: 10.1074/jbc.M702855200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The significance of type II and PrxQ peroxiredoxins for antioxidative stress response in the purple bacterium Rhodobacter sphaeroides.PMID 17644813Read ↗

PrxQ-A, a member of the peroxiredoxin Q family, plays a major role in defense against oxidative stress in the cyanobacterium Anabaena sp. strain PCC7120.Semantic proximity Read ↗

Peroxiredoxin 1 (Prx1) is a dual-function enzyme by possessing Cys-independent catalase-like activity.Semantic proximity Read ↗

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

Thioredoxin is involved in oxygen-regulated formation of the photosynthetic apparatus of Rhodobacter sphaeroides.Semantic proximity Read ↗

Transcriptomic and Physiological Responses to Oxidative Stress in a Chlamydomonas reinhardtii Glutathione Peroxidase Mutant.Semantic proximity Read ↗

Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.Semantic proximity Read ↗

Selective silencing of 2Cys and type-IIB Peroxiredoxins discloses their roles in cell redox state and stress signaling.Semantic proximity Read ↗

The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response.Semantic proximity Read ↗

Mutation and Mutagenesis of thiol peroxidase of Escherichia coli and a new type of thiol peroxidase family.Semantic proximity Read ↗

Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis.Semantic proximity Read ↗

A novel peroxiredoxin of the plant Sedum lineare is a homologue of Escherichia coli bacterioferritin co-migratory protein (Bcp).Semantic proximity Read ↗

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

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