The mechanism of azide activation of polyphenol oxidase II from tobacco.

• Authors: Chunhua Shi , Qingliang Liu , Ya Dai , Yongshu Xie , Xiaolong Xu
• Languages of publication: EN

Abstracts

EN

So far, azide has been consistently reported to act as an inhibitor of metal enzymes, especially copper proteins. The present work shows that azide can also act as an activator of polyphenol oxidase II (PPO II) from tobacco leaves. From0 the square-wave voltammetry of native PPO II, peroxide-PPO II complex and azide-PPO II complex, the reduction of nitro blue tetrazolium by the enzymes and activation of PPO II by peroxide it follows that the binding of azide to PPO II induces the formation of CuO(2)(2-)Cu in the active site of PPO II from CuO(2)(-)Cu in native PPO II. The reason for azide acting as an activator can be attributed to azide complexing with PPO II, thus inducing the formation of CuO(2)(2-)Cu, which is the active site of the peroxide-PPO II complex in which peroxide plays the role of activator.

Keywords

EN

polyphenol oxidase (PPO); azide activation; peroxide activation; superoxide activation; copper proteins

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2002
• Volume: 49
• Issue: 4
• Pages: 1029-1035

Dates

published

2002

received

2002-08-02

revised

2002-11-13

accepted

2002-12-05

Contributors

author

Chunhua Shi

• Department of Chemistry, University of Science and Technology of China, Hefei, 230026 P. R. China

author

Qingliang Liu

• Department of Chemistry, University of Science and Technology of China, Hefei, 230026 P. R. China

author

Ya Dai

• Chongqing Tobacco Industrial Corp. Ltd., Chongqing, P. R. China

author

Yongshu Xie

• Department of Chemistry, University of Science and Technology of China, Hefei, 230026 P. R. China

author

Xiaolong Xu

• Department of Chemistry, University of Science and Technology of China, Hefei, 230026 P. R. China

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