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Article

Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p.

The Journal of biological chemistry - 16 Oct 2009

Ang Swee Kim, Lu Hui

Abstract excerpt

Erv1p is a FAD-dependent sulfhydryl oxidase of the mitochondrial intermembrane space. It contains three conserved disulfide bonds arranged in two CXXC motifs and one CX(16)C motif. Experimental evidence for the specific roles of the individual disulfide bonds is lacking. In this study, structural and functional roles of the disulfides were dissected systematically using a wide range of biochemical and biophysical...

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Share to Catalytic Domain
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Oxidoreductases Acting on Sulfur Group Donors

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Source

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Identifiers

PMID: 19679655
DOI: 10.1074/jbc.M109.021113
PMCID: PMC2781421

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.

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Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p.PMID 19679655Read ↗

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