Proteomics

Dataset Information

0

Characterization of the proteome of human cytochrome c oxidase assembly factors - Experiment A

ABSTRACT: Mitochondrial cytochrome c oxidase (CcO) or respiratory chain complex IV is a heme aa3-copper oxygen reductase containing metal centers essential for holo-complex biogenesis and enzymatic function that are assembled by subunit-specific metallochaperones. The enzyme has two copper sites located in the catalytic core subunits. The COX1 subunit harbors the CuB site that tightly associates with heme a3 while the COX2 subunit contains the binuclear CuA site. Here, we report that in human cells the CcO copper chaperones form macromolecular assemblies and cooperate with several twin CX9C proteins to control heme a biosynthesis and coordinate copper transfer sequentially to the CuA and CuB sites. These data on CcO illustrate a mechanism that regulates the biogenesis of macromolecular enzymatic assemblies with several catalytic metal redox centers and prevents the accumulation of cytotoxic reactive assembly intermediates. We characterized the proteome of COX11, COX19 and PET191 by AP + LC-MS-MS

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Antonio Barrientos  

LAB HEAD: Antonio Barrientos

PROVIDER: PXD034576 | Pride | 2022-08-12

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
Description_MS_Experiments.docx Other
QEp19-1167_Nyvltova_IgG-_1_.mzid.gz Mzid
QEp19-1167_Nyvltova_IgG-_1_.mzid_QEp19-1167_Nyvltova_IgG-_1_.MGF Mzid
QEp19-1167_Nyvltova_IgG.raw Raw
QEp19-1172_Nyvltova_11-_1_.mzid.gz Mzid
Items per page:
1 - 5 of 14
altmetric image

Publications

Coordination of metal center biogenesis in human cytochrome c oxidase.

Nývltová Eva E   Dietz Jonathan V JV   Seravalli Javier J   Khalimonchuk Oleh O   Barrientos Antoni A  

Nature communications 20220624 1

Mitochondrial cytochrome c oxidase (CcO) or respiratory chain complex IV is a heme aa<sub>3</sub>-copper oxygen reductase containing metal centers essential for holo-complex biogenesis and enzymatic function that are assembled by subunit-specific metallochaperones. The enzyme has two copper sites located in the catalytic core subunits. The COX1 subunit harbors the Cu<sub>B</sub> site that tightly associates with heme a<sub>3</sub> while the COX2 subunit contains the binuclear Cu<sub>A</sub> site  ...[more]

Similar Datasets

Proteomics Characterization of the proteome of human cytochrome c oxidase assembly factors - Experiment B
2022-08-12 | PXD034578 | Pride
Proteomics Characterization of the proteome of human cytochrome c oxidase assembly factors - Experiment C
2022-08-12 | PXD034579 | Pride
Proteomics Characterization of the proteome of human cytochrome c oxidase assembly factors - Experiment D
2022-08-12 | PXD034577 | Pride
Proteomics Mitochondrial COA7 is a heme-binding protein with disulfide reductase activity, which is involved in the early stages of complex IV assembly
2022-03-23 | PXD031589 | Pride
Transcriptomics Expression data in BEAS-2B cells and HCT116 cells incubated with copper(II) for different times
2018-11-06 | GSE109375 | GEO
Proteomics HEK293T Coa6 knockout mitochondria
2016-07-28 | PXD001958 | Pride
Transcriptomics The effect of CuO nanoparticles on gene expression patterns in Daphnia magna
2014-03-01 | E-GEOD-54738 | biostudies-arrayexpress
Transcriptomics The effect of ZnO nanoparticles on gene expression patterns in Daphnia magna
2014-03-01 | E-GEOD-54736 | biostudies-arrayexpress
Transcriptomics Role of an archaeal PitA transporter in the copper and arsenic resistance of Metallosphaera sedula an extreme thermoacidophile
2014-07-10 | GSE59253 | GEO
Transcriptomics The role of Salmonella Genomic Island 4 in metal tolerance of Salmonella enterica serovar I 4,[5],12:i:- pork outbreak isolate USDA15WA-1
2020-12-08 | GSE159054 | GEO