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. 2011 Aug 6;2(7):531–542. doi: 10.1007/s13238-011-1079-1

Thiabendazole inhibits ubiquinone reduction activity of mitochondrial respiratory complex II via a water molecule mediated binding feature

Qiangjun Zhou 1,2, Yujia Zhai 1, Jizhong Lou 1, Man Liu 1, Xiaoyun Pang 1, Fei Sun 1,✉
PMCID: PMC4875242  PMID: 21822798

Abstract

The mitochondrial respiratory complex II or succinate: ubiquinone oxidoreductase (SQR) is a key membrane complex in both the tricarboxylic acid cycle and aerobic respiration. Five disinfectant compounds were investigated with their potent inhibition effects on the ubiquinone reduction activity of the porcine mitochondrial SQR by enzymatic assay and crystallography. Crystal structure of the SQR bound with thiabendazole (TBZ) reveals a different inhibitor-binding feature at the ubiquinone binding site where a water molecule plays an important role. The obvious inhibitory effect of TBZ based on the biochemical data (IC50 ∼100 μmol/L) and the significant structure-based binding affinity calculation (∼94 μmol/L) draw the suspicion of using TBZ as a good disinfectant compound for nematode infections treatment and fruit storage.

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Supplementary material is available for this article at 10.1007/s13238-011-1079-1 and is accessible for authorized users.

Keywords: mitochondrial respiratory complex II, thiabendazole, pentachlorophenol, inhibition, crystallography

Electronic supplementary material

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Supplementary material, approximately 888 KB.

Footnotes

Electronic Supplementary Material

Supplementary material is available for this article at 10.1007/s13238-011-1079-1 and is accessible for authorized users.

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