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The cytotoxic lipid peroxidation product, 4‐hydroxy‐2‐nonenal, specifically inhibits decarboxylating dehydrogenases in the matrix of plant mitochondria
Author(s) -
Millar A.Harvey,
Leaver Christopher J
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01976-1
Subject(s) - biochemistry , lipid peroxidation , chemistry , lipoic acid , mitochondrion , nadh dehydrogenase , enzyme , antioxidant , mitochondrial dna , gene
4‐Hydroxy‐2‐nonenal (HNE), a cytotoxic product of lipid peroxidation, inhibits O 2 consumption by potato tuber mitochondria. 2‐Oxoglutarate dehydrogenase (OGDC), pyruvate dehydrogenase complex (PDC) (both 80% inhibited) and NAD‐malic enzyme (50% inhibited) are its major targets. Mitochondrial proteins identified by reaction with antibodies raised to lipoic acid lost this antigenicity following HNE treatment. These proteins were identified as acetyltransferases of PDC (78 kDa and 55 kDa), succinyltransferases of OGDC (50 kDa and 48 kDa) and glycine decarboxylase H protein (17 kDa). The significance of the effect of these inhibitions on the impact of lipid peroxidation and plant respiratory functions is discussed.