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4-Hydroxynonenal and 4-Oxononenal Differentially Bind to the Redox Sensor MitoNEET.

ABSTRACT: MitoNEET is a CDGSH iron-sulfur protein that has been a target for drug development for diseases such as type-2 diabetes, cancer, and Parkinson's disease. Functions proposed for mitoNEET are as a redox sensor and regulator of free iron in the mitochondria. We have investigated the reactivity of mitoNEET toward the reactive electrophiles 4-hydroxynonenal (HNE) and 4-oxononenal (ONE) that are produced from the oxidation of polyunsaturated fatty acid during oxidative stress. Proteomic, electrophoretic, and spectroscopic analysis has shown that HNE and ONE react in a sequence selective manner that was unexpected considering the structure similarity of these two reactive electrophiles.

SUBMITTER: Arnett D

PROVIDER: S-EPMC7556333 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature

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4-Hydroxynonenal and 4-Oxononenal Differentially Bind to the Redox Sensor MitoNEET.

Arnett Dayna D Quillin Alexandria A Geldenhuys Werner J WJ Menze Michael A MA Konkle Mary M

Chemical research in toxicology 20190529 6

MitoNEET is a CDGSH iron-sulfur protein that has been a target for drug development for diseases such as type-2 diabetes, cancer, and Parkinson's disease. Functions proposed for mitoNEET are as a redox sensor and regulator of free iron in the mitochondria. We have investigated the reactivity of mitoNEET toward the reactive electrophiles 4-hydroxynonenal (HNE) and 4-oxononenal (ONE) that are produced from the oxidation of polyunsaturated fatty acid during oxidative stress. Proteomic, electrophore ...[more]

PMID: 31117349

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