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Platanetin and 7‐iodo‐acridone‐4‐carboxylic acid are not specific inhibitors of respiratory NAD(P)H dehydrogenases in potato tuber mitochondria
Author(s) -
Roberts Thomas H.,
Rasmusson Allan G.,
Møller Ian M.
Publication year - 1996
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1996.tb00212.x
Subject(s) - nad+ kinase , submitochondrial particle , rotenone , mitochondrion , biochemistry , respiratory chain , nadh dehydrogenase , dehydrogenase , electron transport chain , glycerol 3 phosphate dehydrogenase , biology , chemistry , enzyme , protein subunit , gene
Progress in understanding the role of NAD(P)H oxidation in plant respiration is restricted by the lack of access to specific inhibitors of each of the unknown number of NAD(P)H dehydrogenases in the inner mitochondrial membrane. Platanetin (3,5,7,8‐tetrahydroxy‐6‐isoprenyl flavone) is known to be an inhibitor of extermal NADH oxidation by plant mitochondria, while 7‐iodo‐acridone‐4‐carboxylic acid (IACA) is an inhibitor of an internal, rotenone‐insensitive NAD(P)H dehydrogenase isolated from yeast mitochondria. Here we show that platanetin inhibits external NAD(P)H oxidation by intact potato ( Solanum tuberosum L. cv. Bintje) tuber mitochondria, deamino‐NADH oxidation by Complex I assayed using inside‐out submitochondrial particles from these mitochondria, and rotenone‐insensitive NAD(P)H oxidation by these submitochondrial particles. IACA was found to inhibit the oxidation of external NADH and succinate by intact mitochondria with similar efficiency. However, IACA also inhibited NADPH and duroquinol oxidation by intact mitochondria as well as deamino‐NADH and NAD(P)H oxidation by inside‐out submitochondrial particles. This indicates that IACA has several sites of inhibition in the electron transport chain. The lack of specificity of both platanetin and IACA prevents these inhibitors from being used to shed more light on the identity of the NAD(P)H dehydrogenases in plant mitochondria.