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• W1978010198 endingPage "41" @default.
• W1978010198 startingPage "33" @default.
• W1978010198 abstract "Hydrogenases catalyze the conversion between 2H+ + 2e− and H2. Most of these enzymes are inhibited by O2, which represents a major drawback for their use in biotechnological applications. Improving hydrogenase O2 tolerance is therefore a major contemporary challenge to allow the implementation of a sustainable hydrogen economy. A few bacteria, however, contain hydrogenases that activate H2 even in the presence of O2. Intriguingly, kinetic and spectroscopic studies lead to assuming that different mechanisms might be responsible for the resistance, depending on the enzyme type. The various hypotheses that emerged from these studies are still a matter of debate. In order to better understand the molecular bases of resistance to O2 inhibition, we explored different methods to improve the O2-tolerance of the O2-sensitive [Ni–Fe] hydrogenase from Desulfovibrio fructosovorans. A whole bunch of mutants has been studied and fully characterized, which revealed that actually, different mechanisms can lead to O2 tolerance. These mechanisms are described in this review and compared to the current hypothesis of O2 tolerance." @default.
• W1978010198 created "2016-06-24" @default.
• W1978010198 creator A5040444990 @default.
• W1978010198 creator A5053466535 @default.
• W1978010198 creator A5069606617 @default.
• W1978010198 creator A5085019976 @default.
• W1978010198 date "2011-01-01" @default.
• W1978010198 modified "2023-09-25" @default.
• W1978010198 title "Towards engineering O₂-tolerance in [Ni–Fe] hydrogenases" @default.
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