Open Access4-Hydroxynonenal and 4-Oxononenal Differentially Bind to the Redox Sensor MitoNEET
Author(s) -
Dayna Ann Maria Arnett,
Alexandria Quillin,
Werner J. Geldenhuys,
Michael A. Menze,
Mary E. Konkle
Publication year - 2019
Publication title -
chemical research in toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.031
H-Index - 156
eISSN - 1520-5010
pISSN - 0893-228X
DOI - 10.1021/acs.chemrestox.9b00166
Subject(s) - 4 hydroxynonenal , redox , chemistry , electrophile , oxidative stress , mitochondrion , regulator , biochemistry , oxidation reduction , reactive oxygen species , reactivity (psychology) , biophysics , biology , gene , lipid peroxidation , medicine , alternative medicine , organic chemistry , pathology , catalysis
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.