No role of DT-diaphorase (NQO1) in the protection against oxidized quercetin

A.W. Boots; A. Bast; G.R. Haenen

doi:10.1016/j.febslet.2004.12.044

No role of DT-diaphorase (NQO1) in the protection against oxidized quercetin

A.W. Boots^*, A. Bast, G.R. Haenen

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Quercetin is one of the most studied alimentary antioxidants. During its antioxidant activity, quercetin becomes oxidized into its ortho-quinone/quinone methide, denoted as QQ. QQ is toxic since it is highly reactive towards thiols. DT-diaphorase (NQO1) might protect against QQ toxicity by reducing QQ to quercetin. However, conflicting data have been reported. The aim of the present study is to elucidate the role of DT-diaphorase in the protection against QQ-mediated thiol reactivity. It was found that QQ is indeed a substrate for DT-diaphorase. However, QQ reacted much faster with glutathione or protein thiols than with DT-diaphorase in experiments with isolated compounds as well as with human liver cytosol or blood plasma. This indicates that DT-diaphorase has no role in the protection against QQ.

Original language	English
Pages (from-to)	677-682
Journal	Febs Letters
Volume	579
Issue number	3
DOIs	https://doi.org/10.1016/j.febslet.2004.12.044
Publication status	Published - 1 Jan 2005

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10.1016/j.febslet.2004.12.044

Cite this

@article{526c7f0457274bde808a5989478672b5,

title = "No role of DT-diaphorase (NQO1) in the protection against oxidized quercetin",

abstract = "Quercetin is one of the most studied alimentary antioxidants. During its antioxidant activity, quercetin becomes oxidized into its ortho-quinone/quinone methide, denoted as QQ. QQ is toxic since it is highly reactive towards thiols. DT-diaphorase (NQO1) might protect against QQ toxicity by reducing QQ to quercetin. However, conflicting data have been reported. The aim of the present study is to elucidate the role of DT-diaphorase in the protection against QQ-mediated thiol reactivity. It was found that QQ is indeed a substrate for DT-diaphorase. However, QQ reacted much faster with glutathione or protein thiols than with DT-diaphorase in experiments with isolated compounds as well as with human liver cytosol or blood plasma. This indicates that DT-diaphorase has no role in the protection against QQ.",

author = "A.W. Boots and A. Bast and G.R. Haenen",

year = "2005",

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doi = "10.1016/j.febslet.2004.12.044",

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journal = "Febs Letters",

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TY - JOUR

T1 - No role of DT-diaphorase (NQO1) in the protection against oxidized quercetin

AU - Boots, A.W.

AU - Bast, A.

AU - Haenen, G.R.

PY - 2005/1/1

Y1 - 2005/1/1

N2 - Quercetin is one of the most studied alimentary antioxidants. During its antioxidant activity, quercetin becomes oxidized into its ortho-quinone/quinone methide, denoted as QQ. QQ is toxic since it is highly reactive towards thiols. DT-diaphorase (NQO1) might protect against QQ toxicity by reducing QQ to quercetin. However, conflicting data have been reported. The aim of the present study is to elucidate the role of DT-diaphorase in the protection against QQ-mediated thiol reactivity. It was found that QQ is indeed a substrate for DT-diaphorase. However, QQ reacted much faster with glutathione or protein thiols than with DT-diaphorase in experiments with isolated compounds as well as with human liver cytosol or blood plasma. This indicates that DT-diaphorase has no role in the protection against QQ.

AB - Quercetin is one of the most studied alimentary antioxidants. During its antioxidant activity, quercetin becomes oxidized into its ortho-quinone/quinone methide, denoted as QQ. QQ is toxic since it is highly reactive towards thiols. DT-diaphorase (NQO1) might protect against QQ toxicity by reducing QQ to quercetin. However, conflicting data have been reported. The aim of the present study is to elucidate the role of DT-diaphorase in the protection against QQ-mediated thiol reactivity. It was found that QQ is indeed a substrate for DT-diaphorase. However, QQ reacted much faster with glutathione or protein thiols than with DT-diaphorase in experiments with isolated compounds as well as with human liver cytosol or blood plasma. This indicates that DT-diaphorase has no role in the protection against QQ.

U2 - 10.1016/j.febslet.2004.12.044

DO - 10.1016/j.febslet.2004.12.044

M3 - Article

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