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

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

Biochimie - 1 Sept 2018

Fox Nicholas G, Martelli Alain, Nabhan Joseph F, Janz Jay, Borkowska Oktawia, Bulawa Christine, Yue Wyatt W

Abstract excerpt

Human de novo iron-sulfur (Fe-S) assembly complex consists of cysteine desulfurase NFS1, accessory protein ISD11, acyl carrier protein ACP, scaffold protein ISCU, and allosteric activator frataxin (FXN). FXN binds the NFS1-ISD11-ACP-ISCU complex (SDAU), to activate the desulfurase activity and Fe-S cluster biosynthesis. In the absence of FXN, the NFS1-ISD11-ACP (SDA) complex was reportedly inhibited by binding of...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Carbon-Sulfur Lyases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Frataxin

Share to Iron-Binding Proteins

Share to Iron-Sulfur Proteins

Share to Methionine

Share to Recombinant Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 30031876
DOI: 10.1016/j.biochi.2018.07.012
PMCID: PMC6098246

Genes

ISCU
FXN
NFS1

Variants

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

Zinc(II) binding on human wild-type ISCU and Met140 variants modulates NFS1 desulfurase activity.PMID 30031876Read ↗

Zinc(II) binding on human wild-type ISCU and Met140 variants modulates Fe-S complex activitySemantic proximity Read ↗

Structure of the human frataxin-bound iron-sulfur cluster assembly complex provides insight into its activation mechanismSemantic proximity Read ↗

Recapitulating the frataxin activation mechanism in an engineered bacterial cysteine desulfurase supports the architectural switch modelSemantic proximity Read ↗

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

Iron binding activity is essential for the function of IscA in iron-sulphur cluster biogenesis.Semantic proximity Read ↗

Analysis of NFU-1 metallocofactor binding-site substitutions-impacts on iron-sulfur cluster coordination and protein structure and function.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 ↗

Mammalian mitochondrial iron–sulfur cluster biogenesis and transfer and related human diseasesSemantic proximity Read ↗

Mutations in LYRM4, encoding iron-sulfur cluster biogenesis factor ISD11, cause deficiency of multiple respiratory chain complexes.Semantic proximity Read ↗

Iron-sulfur cluster biosynthesis and trafficking - impact on human disease conditions.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 ↗

Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly.Semantic proximity Read ↗

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