In fact, as the team reports, the setup increased the efficiency of H2 production 100-fold over previous attempts
with hydrogenases.
Not exact matches
But
with microbes, it is possible to intervene genetically in ways that encourage the activation of
hydrogenase enzymes.
The researchers then spiked their solution
with protons and electron - ferrying molecules, which were able to diffuse into the spheres, where the
hydrogenase pairs readily converted them into H2.
When they put it all together and infected salmonella bacteria
with the remade viruses, the new guide proteins helped assemble the spheres and inserted roughly 100 copies of the
hydrogenase into the interior of each one.
The scientists came up
with a surprisingly simple ligand structure resembling natural
hydrogenase enzymes
with a twist from typical phosphine catalysts.
In nature, hydrogen (H2) molecules store energy and release it as needed
with the aid of
hydrogenase enzymes.
Because the
hydrogenases found in nature don't last as long as ones that are built out of tougher chemicals (think paper versus plastic), the researchers wanted to pull out the active portion of the biological
hydrogenase and redesign it
with a stable chemical backbone.
The program focuses on development of transition - metal complexes that are inspired by the natural photosynthetic enzymes such as nitrogenases,
hydrogenases, and the oxygen - evolving complex of photosystem II
with the goal of designing catalysts that are chemically stable, active, and highly selective for specific chemical targets.