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

Abstract:

: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. From 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.

journal_name

Acta Biochim Pol

journal_title

Acta biochimica Polonica

authors

Shi C,Liu Q,Dai Y,Xie Y,Xu X

doi

0249041029

subject

Has Abstract

pub_date

2002-01-01 00:00:00

pages

1029-35

issue

4

eissn

0001-527X

issn

1734-154X

journal_volume

49

pub_type

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