Hydrogen-Activating Enzymes: Activity Does Not Correlate with Oxygen Sensitivity

• Published in: Angewandte Chemie (International ed.) Vol. 47; no. 11; pp. 2052 - 2054
• Main Authors: Baffert, Carole, Demuez, Marie, Cournac, Laurent, Burlat, Bénédicte, Guigliarelli, Bruno, Bertrand, Patrick, Girbal, Laurence, Léger, Christophe
• Format: Journal Article
• Language: English
• Published: Weinheim Wiley-VCH Verlag 01.01.2008; WILEY-VCH Verlag; WILEY‐VCH Verlag
• Subjects: Binding Sites; Electrodes; electron transfer; Enzyme Activation; Hydrogen - chemistry; Hydrogenase - chemistry; hydrogenases; inhibition; kinetics; Oxygen - chemistry; Protein Conformation; protein film voltammetry; Sensitivity and Specificity; Time Factors
• ISSN: 1433-7851; 1521-3773
• DOI: 10.1002/anie.200704313

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.