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

Identification of an essential cysteinyl residue in the ArsC arsenate reductase of plasmid R773.

Biochemistry - 17 Oct 1995

Liu J, Gladysheva T B, Lee L, Rosen B P

Abstract excerpt

The ArsC protein encoded by the arsenical resistance operon of plasmid R773 catalyzes the reduction of arsenate to arsenite in Escherichia coli. The reductase has been shown to require glutathione and glutaredoxin, suggesting that thiol chemistry might be involved in the reaction mechanism. The ArsC arsenate reductase has two cysteinyl residues, Cys12 and Cys106. By a combination of random and site-specific...

Read the complete abstract on PubMed

Topics

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

Share to Drug Resistance, Microbial
Share to Escherichia coli
Share to Genes, Bacterial

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Genotype

Share to Kinetics

Share to Mutagenesis, Site-Directed

Share to Phenotype

Share to Recombinant Proteins

Source

Identifiers

PMID: 7577935
DOI: 10.1021/bi00041a026

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of an essential cysteinyl residue in the ArsC arsenate reductase of plasmid R773.PMID 7577935Read ↗

The phosphatase C(X)5R motif is required for catalytic activity of the Saccharomyces cerevisiae Acr2p arsenate reductase.Semantic proximity Read ↗

Identification of a putative metal binding site in a new family of metalloregulatory proteins.Semantic proximity Read ↗

Role of vicinal cysteine pairs in metalloid sensing by the ArsD As(III)-responsive repressor.Semantic proximity Read ↗

Arsenic binding and transfer by the ArsD As(III) metallochaperone.Semantic proximity Read ↗

Cys-113 and Cys-422 form a high affinity metalloid binding site in the ArsA ATPase.Semantic proximity Read ↗

Genetic mapping of the interface between the ArsD metallochaperone and the ArsA ATPase.Semantic proximity Read ↗

Thioredoxin or glutaredoxin in Escherichia coli is essential for sulfate reduction but not for deoxyribonucleotide synthesis.Semantic proximity Read ↗

Analysis of the ars gene cluster from highly arsenic-resistant Burkholderia xenovorans LB400.Semantic proximity Read ↗

Mutagenesis of a nucleotide-binding site of an anion-translocating ATPase.Semantic proximity Read ↗

Bifunctional protein ArsRM contributes to arsenite methylation and resistance in Brevundimonas sp. M20Semantic proximity Read ↗

The ArsR repressor mediates arsenite-dependent regulation of arsenate respiration and detoxification operons of Shewanella sp. strain ANA-3.Semantic proximity Read ↗

The sac mutants of Chlamydomonas reinhardtii reveal transcriptional and posttranscriptional control of cysteine biosynthesis.Semantic proximity Read ↗

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