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Ferulenol specifically inhibits succinate ubiquinone reductase at the level of the ubiquinone cycle.

Abstract：

:The natural compound ferulenol, a sesquiterpene prenylated coumarin derivative, was purified from Ferula vesceritensis and its mitochondrial effects were studied. Ferulenol caused inhibition of oxidative phoshorylation. At low concentrations, ferulenol inhibited ATP synthesis by inhibition of the adenine nucleotide translocase without limitation of mitochondrial respiration. At higher concentrations, ferulenol inhibited oxygen consumption. Ferulenol caused specific inhibition of succinate ubiquinone reductase without altering succinate dehydrogenase activity of the complex II. This inhibition results from a limitation of electron transfers initiated by the reduction of ubiquinone to ubiquinol in the ubiquinone cycle. This original mechanism of action makes ferulenol a useful tool to study the physiological role and the mechanism of electron transfer in the complex II. In addition, these data provide an additional mechanism by which ferulenol may alter cell function and demonstrate that mitochondrial dysfunction is an important determinant in Ferula plant toxicity.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Lahouel M,Zini R,Zellagui A,Rhouati S,Carrupt PA,Morin D

doi

10.1016/j.bbrc.2007.01.145

subject

Has Abstract

pub_date

2007-03-30 00:00:00

pages

252-7

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)00212-4

journal_volume

355

pub_type

杂志文章

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