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

doi:10.1016/j.bbrc.2007.01.145

Title: Ferulenol specifically inhibits succinate ubiquinone reductase at the level of the ubiquinone cycle

Full Record
Similar

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.

Authors:

Lahouel, Mesbah ^[1]; Zini, Roland ^[2]; Universite Paris 12, Faculte de Medecine, Laboratoire de Pharmacologie, Creteil F-94010 ^[3]; Zellagui, Ammar ^[4]; Rhouati, Salah ^[4]; Carrupt, Pierre-Alain ^[5]; Morin, Didier ^[2]; Universite Paris 12, Faculte de Medecine, Laboratoire de Pharmacologie, Creteil F-94010 ^[3]; E-mail: didier.morin@creteil.inserm.fr

Departement de pharmacologie et phytochimie, Universite de Jijel (Algeria)
INSERM U841, Creteil F-94010 (France)
(France)
Laboratoire des substances naturelles, Universite de Constantine (Algeria)
LCT-Pharmacochimie, Section des Sciences Pharmaceutiques, Universite de Geneve (Switzerland)

Publication Date:: Fri Mar 30 00:00:00 EDT 2007

OSTI Identifier:: 20979861

Resource Type:: Journal Article

Resource Relation:: Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 355; Journal Issue: 1; Other Information: DOI: 10.1016/j.bbrc.2007.01.145; PII: S0006-291X(07)00212-4; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)

Country of Publication:: United States

Language:: English

Subject:: 60 APPLIED LIFE SCIENCES; ADENINES; ATP; BIOSYNTHESIS; COMPLEXES; COUMARIN; ELECTRON TRANSFER; INHIBITION; MITOCHONDRIA; OXIDATION; OXYGEN; PHOSPHORYLATION; RESPIRATION; TOXICITY; UBIQUINONE

Citation Formats


                    Lahouel, Mesbah, Zini, Roland, Universite Paris 12, Faculte de Medecine, Laboratoire de Pharmacologie, Creteil F-94010, Zellagui, Ammar, Rhouati, Salah, Carrupt, Pierre-Alain, Morin, Didier, Universite Paris 12, Faculte de Medecine, Laboratoire de Pharmacologie, Creteil F-94010, and E-mail: didier.morin@creteil.inserm.fr. Ferulenol specifically inhibits succinate ubiquinone reductase at the level of the ubiquinone cycle.  United States: N. p., 2007. 
        Web.  doi:10.1016/j.bbrc.2007.01.145.

Copy to clipboard


                    Lahouel, Mesbah, Zini, Roland, Universite Paris 12, Faculte de Medecine, Laboratoire de Pharmacologie, Creteil F-94010, Zellagui, Ammar, Rhouati, Salah, Carrupt, Pierre-Alain, Morin, Didier, Universite Paris 12, Faculte de Medecine, Laboratoire de Pharmacologie, Creteil F-94010, & E-mail: didier.morin@creteil.inserm.fr. Ferulenol specifically inhibits succinate ubiquinone reductase at the level of the ubiquinone cycle.  United States.  doi:10.1016/j.bbrc.2007.01.145.

Copy to clipboard


                    Lahouel, Mesbah, Zini, Roland, Universite Paris 12, Faculte de Medecine, Laboratoire de Pharmacologie, Creteil F-94010, Zellagui, Ammar, Rhouati, Salah, Carrupt, Pierre-Alain, Morin, Didier, Universite Paris 12, Faculte de Medecine, Laboratoire de Pharmacologie, Creteil F-94010, and E-mail: didier.morin@creteil.inserm.fr. Fri .  
        "Ferulenol specifically inhibits succinate ubiquinone reductase at the level of the ubiquinone cycle".  United States.  
        doi:10.1016/j.bbrc.2007.01.145.

Copy to clipboard


                    
@article{osti_20979861,

  title        = {Ferulenol specifically inhibits succinate ubiquinone reductase at the level of the ubiquinone cycle},

  author       = {Lahouel, Mesbah and Zini, Roland and Universite Paris 12, Faculte de Medecine, Laboratoire de Pharmacologie, Creteil F-94010 and Zellagui, Ammar and Rhouati, Salah and Carrupt, Pierre-Alain and Morin, Didier and Universite Paris 12, Faculte de Medecine, Laboratoire de Pharmacologie, Creteil F-94010 and E-mail: didier.morin@creteil.inserm.fr},

  abstractNote = {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.},

  doi          = {10.1016/j.bbrc.2007.01.145},

  journal      = {Biochemical and Biophysical Research Communications},

  number       = 1,

  volume       = 355,

  place        = {United States},

  year         = {Fri Mar 30 00:00:00 EDT 2007},

  month        = {Fri Mar 30 00:00:00 EDT 2007}

}

Copy to clipboard

Journal Article:

DOI: 10.1016/j.bbrc.2007.01.145

Other availability

Find in Google Scholar

Search WorldCat to find libraries that may hold this journal

Save / Share:

Export Metadata

Save to My Library

Multi-level regulation of the chloroplast ATP synthase: the chloroplast NADPH thioredoxin reductase C (NTRC) is required for redox modulation specifically under low irradiance

Carrillo, L. Ruby ; Froehlich, John E. ; Cruz, Jeffrey A. ; ... - The Plant Journal
Cited by 11
DOI: 10.1111/tpj.13226
Inhibition of NADH-ubiquinone reductase activity by N,N'-dicyclohexylcarbodiimide and correlation of this inhibition with the occurrence of energy-coupling site 1 in various organisms

Yagi, T. - Biochemistry; (United States)

The NADH-ubiquinone reductase activity of the respiratory chains of several organisms was inhibited by the carboxyl-modifying reagent N,N'-dicyclohexylcarbodiimide (DCCD). This inhibition correlated with the presence of an energy-transducing site in this segment of the respiratory chain. Where the NADH-quinone reductase segment involved an energy-coupling site (e.g., in bovine heart and rat liver mitochondria, and in Paracoccus denitrificans, Escherichia coli, and Thermus thermophilus HB-8 membranes), DCCD acted as an inhibitor of ubiquinone reduction by NADH. By contrast, where energy-coupling site 1 was absent (e.g., in Saccharomyces cerevisiae mitochondria and BacilLus subtilis membranes), there was no inhibition of NADH-ubiquinone reductase activity bymore »« less
INHIBITION BY X-RAYS OF THE EFFECT OF SUCCINATE CYTOCHROME C REDUCTASE ON MITOCHONDRIA IN AN IN VITRO CULTIVATED EMBRYONIC CHICKEN ORGAN. (in French)

Gasc, J.M. - Compt. Rend., Ser. D 274: No. 5, 723-5(31 Jan 1972).
INHIBITION PRODUCED BY X-RAYS AND THE RADIOPROTECTION QUALITIES OF SUCCINATE CYTOCHROME C REDUCTASE THAM IN THE MITOCHONDRIES OF AN EMBRYONIC ORGAN. (in French)

Reinbold, M. ; Gasc, J.M. - Compt. Rend., Ser. D 274: No. 6, 932-5(7 Feb 1972).
Internal electron transfer within mitochondrial succinate-cytochrome C reductase

Ilan, Y. - Biochem. Biophys. Res. Commun.; (United States)

Internal electron transfer within succinate-cytochrome C reductase from pigeon breast muscle mitochondria was followed by the pulse radiolytic technique. The electron equivalent is transferred from an unknown donor to b type cytochrome(s), in a first order process with a rate constant of: 660 +- 150s/sup -1/. This process might be the rate determining step of electron transfer in mitochondria, since it is similar in rate to the turnover number of the mitochondrial respiratory chain.
DOI: 10.1016/0006-291X(78)91139-7