BLOOMINGTON, Ind. -- 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.
"Essentially, we've taken a virus's ability to self-assemble myriad genetic building blocks and incorporated a very fragile and sensitive enzyme with the remarkable property of taking in protons and spitting out hydrogen gas," said Trevor Douglas, the Earl Blough Professor of Chemistry in the IU Bloomington College of Arts and Sciences' Department of Chemistry, who led the study. "The end result is a virus-like particle that behaves the same as a highly sophisticated material that catalyzes the production of hydrogen."
Other IU scientists who contributed to the research were Megan C. Thielges, an assistant professor of chemistry; Ethan J. Edwards, a Ph.D. student; and Paul C. Jordan, a postdoctoral researcher at Alios BioPharma, who was an IU Ph.D. student at the time of the study.
The genetic material used to create the enzyme, hydrogenase, is produced by two genes from the common bacteria Escherichia coli, inserted inside the protective capsid using methods previously developed by these IU scientists. The genes, hyaA and hyaB, are two genes in E. coli that encode key subunits of the hydrogenase enzyme. The capsid comes from the bacterial virus known as bacteriophage P22.
The resulting biomaterial, called "P22-Hyd," is not only more efficient than the unaltered enzyme but also is produced through a simple fermentation process at room temperature.