Date: 13.8.2013
Researchers at the Ruhr-Universität Bochum (RUB) have discovered an efficient process for hydrogen biocatalysis. They developed semi-synthetic hydrogenases, hydrogen-generating enzymes.
These enzymes were created by adding the protein's biological precursor to a chemically synthesized inactive iron complex. From these two components, the biological catalyst formed spontaneously in a test tube.
"Extracting hydrogenases from living cells is highly difficult," says Prof Dr Thomas Happe, head of the work group Photobiotechnology at the RUB. "Therefore, their industrial application has always been a long way off. Now, we have made a decisive step towards the generation of bio-based materials." Together with colleagues from the MPI Mülheim and from Grenoble, the RUB researchers report their findings in the journal Nature Chemical Biology.
"Under ideal conditions, one single hydrogenase enzyme can generate 9,000 hydrogen molecules per second," says Thomas Happe. "Nature has created a catalyst that is incredibly active even without any rare noble metals." The researchers from Bochum examine so-called iron-iron [FeFe] hydrogenases whose catalysis is based on an active centre with a complex structure that contains iron, carbon monoxide and cyanide – only few living organisms are able to synthesize it.
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