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A function for novel uncoupling proteins: antioxidant defense of mitochondrial matrix by translocating fatty acid peroxides from the inner to the outer membrane leaflet
Author(s) -
Goglia Fernando,
Skulachev Vladimir P.
Publication year - 2003
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.03-0159hyp
Subject(s) - inner mitochondrial membrane , inner membrane , mitochondrial carrier , mitochondrion , mitochondrial matrix , bacterial outer membrane , chemistry , fatty acid , biochemistry , translocase of the inner membrane , electron transport chain , membrane potential , microbiology and biotechnology , atp–adp translocase , biophysics , biology , cytosol , mitochondrial membrane transport protein , gene , enzyme , escherichia coli
It is hypothesized that mitochondrial uncoupling proteins operate as carriers of fatty acid peroxide anions. This is assumed to result in electrophoretic extrusion of such anions from the inner to the outer leaflet of the inner mitochondrial membrane, being driven by membrane potential (mitochondrial interior negative). In this way, the inner leaflet is ridded of fatty acid peroxides that otherwise can form very aggressive oxidants damaging mitochondrial DNA, aconitase, and other mitochondrial matrix‐localized components of vital importance. The steady‐state concentration the fatty acid peroxides is known to be low. This explains why UCP2, 3, 4, and 5 are present in small amounts usually insufficient to make a large contribution to the H + conductance of the mitochondrial membrane.—Goglia, F., Skulachev, V. P. A function for novel uncoupling proteins: antioxidant defense of mitochondrial matrix by translocating fatty acid peroxides from the inner to the outer membrane leaflet. FASEB J. 17, 1585–1591 (2003)