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

Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies.

Scientific reports - 17 Dec 2015

Andjelković Ana, Oliveira Marcos T, Cannino Giuseppe, Yalgin Cagri, Dhandapani Praveen K, Dufour Eric, Rustin Pierre, Szibor Marten, Jacobs Howard T

Abstract excerpt

The mitochondrial alternative oxidase, AOX, carries out the non proton-motive re-oxidation of ubiquinol by oxygen in lower eukaryotes, plants and some animals. Here we created a modified version of AOX from Ciona instestinalis, carrying mutations at conserved residues predicted to be required for chelation of the diiron prosthetic group. The modified protein was stably expressed in mammalian cells or flies, but...

Read the complete abstract on PubMed

Topics

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

Share to Animals, Genetically Modified
Share to Electron Transport Complex IV

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Knockdown Techniques

Share to Mitochondrial Proteins

Share to Oxidoreductases

Share to Oxygen Consumption

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 26672986
DOI: 10.1038/srep18295
PMCID: PMC4682143

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies.PMID 26672986Read ↗

Expression of the Ciona intestinalis alternative oxidase (AOX) in Drosophila complements defects in mitochondrial oxidative phosphorylation.Semantic proximity Read ↗

AOX delays the onset of the lethal phenotype in a mouse model of Uqcrh (complex III) disease.Semantic proximity Read ↗

Expression of alternative oxidase in Drosophila ameliorates diverse phenotypes due to cytochrome oxidase deficiency.Semantic proximity Read ↗

Developmental arrest in Drosophila melanogaster caused by mitochondrial DNA replication defects cannot be rescued by the alternative oxidase.Semantic proximity Read ↗

Ubiquinol-binding site in the alternative oxidase: mutagenesis reveals features important for substrate binding and inhibition.Semantic proximity Read ↗

The alternative oxidase AOX does not rescue the phenotype of tko25t mutant flies.Semantic proximity Read ↗

Towards a structural elucidation of the alternative oxidase in plants.Semantic proximity Read ↗

Systemic impact of the expression of the mitochondrial alternative oxidase on <i>Drosophila</i> developmentSemantic proximity Read ↗

Expression of the alternative oxidase complements cytochrome c oxidase deficiency in human cells.Semantic proximity Read ↗

The alternative oxidase reconfigures the larval mitochondrial electron transport system to accelerate growth and development in <i>Drosophila melanogaster</i>Semantic proximity Read ↗

New insight into the structure and function of the alternative oxidase.Semantic proximity Read ↗

The Oxa2 protein of Neurospora crassa plays a critical role in the biogenesis of cytochrome oxidase and defines a ubiquitous subbranch of the Oxa1/YidC/Alb3 protein family.Semantic proximity Read ↗

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