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

Persulfide formation on mitochondrial cysteine desulfurase: enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis.

The Biochemical journal - 1 Dec 2012

Pandey Alok, Golla Ramesh, Yoon Heeyong, Dancis Andrew, Pain Debkumar

Abstract excerpt

Cysteine desulfurases abstract sulfur from the substrate cysteine, generate a covalent persulfide on the active site cysteine of the enzyme, and then donate the persulfide sulfur to various recipients such as Fe-S clusters. In Saccharomyces cerevisiae, the Nfs1p protein is the only known cysteine...

Read the complete abstract on PubMed

Topics

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

Share to Carbon-Sulfur Lyases
Share to Enzyme Activation
Share to Genes, Fungal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Iron-Sulfur Proteins

Share to Mitochondrial Proteins

Share to Multienzyme Complexes

Share to Sulfides

Share to Sulfurtransferases

Source

Identifiers

PMID: 22928949
DOI: 10.1042/BJ20120951

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22928949-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Persulfide formation on mitochondrial cysteine desulfurase: enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis.PMID 22928949Read ↗

Isd11p protein activates the mitochondrial cysteine desulfurase Nfs1p protein.Semantic proximity Read ↗

Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly.Semantic proximity Read ↗

The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins.Semantic proximity Read ↗

The Fe/S cluster assembly protein Isd11 is essential for tRNA thiolation in Trypanosoma brucei.Semantic proximity Read ↗

Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution.Semantic proximity Read ↗

Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins.Semantic proximity Read ↗

Turning Saccharomyces cerevisiae into a Frataxin-Independent Organism.Semantic proximity Read ↗

The <i>Plasmodium falciparum</i> apicoplast cysteine desulfurase provides sulfur for both iron sulfur cluster assembly and tRNA modificationSemantic proximity Read ↗

AtSufE is an essential activator of plastidic and mitochondrial desulfurases in Arabidopsis.Semantic proximity Read ↗

Molecular basis of function and the unusual antioxidant activity of a cyanobacterial cysteine desulfurase.Semantic proximity Read ↗

Zinc(II) binding on human wild-type ISCU and Met140 variants modulates NFS1 desulfurase activity.Semantic proximity Read ↗

Assembly of the [4Fe-4S] cluster of NFU1 requires the coordinated donation of two [2Fe-2S] clusters from the scaffold proteins, ISCU2 and ISCA1.Semantic proximity Read ↗

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