Scientists at Indiana University have created a highly efficient biomaterial that catalyzes the formation of hydrogen -- one half of the "holy grail" of splitting H2O to make hydrogen and oxygen for fueling cheap and efficient cars that run on water.
A modified enzyme that gains strength from being protected within the protein shell -- or "capsid" -- of a bacterial virus, this new material is 150 times more efficient than the unaltered form of the enzyme.
The process of creating the material was recently reported in "Self-assembling biomolecular catalysts for hydrogen production" in the journal Nature Chemistry.
Ref: Self-assembling biomolecular catalysts for hydrogen production. Nature Chemistry (21 December 2015) | DOI: 10.1038/nchem.2416
The chemistry of highly evolved protein-based compartments has inspired the design of new catalytically active materials that self-assemble from biological components. A frontier of this biodesign is the potential to contribute new catalytic systems for the production of sustainable fuels, such as hydrogen. Here, we show the encapsulation and protection of an active hydrogen-producing and oxygen-tolerant [NiFe]-hydrogenase, sequestered within the capsid of the bacteriophage P22 through directed self-assembly. We co-opted Escherichia coli for biomolecular synthesis and assembly of this nanomaterial by expressing and maturing the EcHyd-1 hydrogenase prior to expression of the P22 coat protein, which subsequently self assembles. By probing the infrared spectroscopic signatures and catalytic activity of the engineered material, we demonstrate that the capsid provides stability and protection to the hydrogenase cargo. These results illustrate how combining biological function with directed supramolecular self-assembly can be used to create new materials for sustainable catalysis.