Hydrogen-activating enzymes:: Activity does not correlate with oxygen sensitivity

被引：87

作者：

Baffert, Carole ^{[1
]}

Demuez, Marie ^{[2
]}

Cournac, Laurent ^{[3
]}

Burlat, Benedicte ^{[1
]}

Guigliarelli, Bruno ^{[1
]}

Bertrand, Patrick ^{[1
]}

Girbal, Laurence ^{[2
]}

Leger, Christophe ^{[1
]}

机构：

[1] Univ Aix Marseille 1, Lab Bioengn & Ingn Prot, CNRS, Marseille, France

[2] INSA, INRA, CNRS, Lab Ingn Syst Biol & Procedes, Toulouse, France

[3] Univ Aix Marseille 2, CNRS, Lab Bioengn & Biotechnol Bacteries & Microalgues, CEA,DSV,IBEB, St Paul Les Durance, France

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2008年 / 47卷 / 11期

关键词：

electron transfer; hydrogenases; inhibition; kinetics; protein film voltammetry;

D O I：

10.1002/anie.200704313

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Surprisingly uninhibited: The inhibition of hydrogenases by oxygen is intensely studied because this is the main obstacle to using these enzymes in biofuel cells. The hydrogenase from Clostridium acetobutylicum (see structure) was found to react surprisingly slowly with O2. The inhibition mechanism was elucidated and the kinetics were quantitatively defined. This is a prerequisite for improving the enzyme further by genetic engineering and for assessing its potential in technological devices. (Figure Presented) © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：2052 / 2054

页数：3

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