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.
"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."
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. The material is potentially far less expensive and more environmentally friendly to produce than other materials currently used to create fuel cells. The costly and rare metal platinum, for example, is commonly used to catalyze hydrogen as fuel in products such as high-end concept cars.
In addition, P22-Hyd both breaks the chemical bonds of water to create hydrogen and also works in reverse to recombine hydrogen and oxygen to generate power. "The reaction runs both ways- it can be used either as a hydrogen production catalyst or as a fuel cell catalyst,"
The form of hydrogenase is one of three occurring in nature: di-iron (FeFe)-, iron-only (Fe-only)- and nitrogen-iron (NiFe)-hydrogenase. The third form was selected for the new material due to its ability to easily integrate into biomaterials and tolerate exposure to oxygen.
NiFe-hydrogenase also gains significantly greater resistance upon encapsulation to breakdown from chemicals in the environment, and it retains the ability to catalyze at room temperature. Unaltered NiFe-hydrogenase, by contrast, is highly susceptible to destruction from chemicals in the environment and breaks down at temperatures above room temperature- both of which make the unprotected enzyme a poor choice for use in manufacturing and commercial products such as cars.