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A modified Fe-S cluster modulates [Ni-Fe] hydrogenase oxidative damage


​IBS researchers have studied the crystal structure of an O2-sensitive variant of an Escherichia coli hydrogenase-1. The results of their computational studies on electron transfer help to explain how the structural and redox properties of the new FeS cluster modulate the observed phenotype.

Published on 1 August 2018
Hydrogenases are enzymes of considerable interest for their potential biotechnological applications both as catalysts in biofuel cells and hydrogen producers. However, these applications can be greatly affected by their reactions with atmospheric oxygen.

In order to better understand this problem, researchers at the IBS investigated a single mutation of the naturally O2-tolerant E. coli [NiFe] hydrogenase-1, which makes it O2-sensitive by changing its [4Fe-3S] cluster into a novel [4Fe-4S] cluster. Their theoretical study explains in detail the observed different redox properties of these two clusters and sheds considerable light on the biological solution to prevent O2-based deactivation.

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