Looking to nature for their muse, researchers have used a common protein to guide the design of a material that can make energy-storing hydrogen gas. The synthetic material works 10 times faster than the original protein found in water-dwelling microbes, the researchers report in the August 12 issue of the journal Science, clocking in at 100,000 molecules of hydrogen gas every second.
The part of the catalyst that cranks out 100,000
molecules of hydrogen gas a second packs electrons
into chemical bonds between hydrogen atoms, possibly
hijacked from water. Credit: PNNL
This step is just one part of a series of reactions to split water and make hydrogen gas, but the researchers say the result shows they can learn from nature how to control those reactions to make durable synthetic catalysts for energy storage, such as in fuel cells.
In addition, the natural protein, an enzyme, uses inexpensive, abundant metals in its design, which the team copied. Currently, these materials -- called catalysts, because they spur reactions along -- rely on expensive metals such as platinum.
"This nickel-based catalyst is really very fast," said coauthor Morris Bullock of the Department of Energy's Pacific Northwest National Laboratory. "It's about a hundred times faster than the previous catalyst record holder. And from nature, we knew it could be done with abundant and inexpensive nickel or iron."
Stuffing Bonds
Electrical energy is nothing more than electrons. These same electrons are what tie atoms together when they are chemically bound to each other in molecules such as hydrogen gas. Stuffing electrons into chemical bonds is one way to store electrical energy, which is particularly important for renewable, sustainable energy sources like solar or wind power. Converting the chemical bonds back into flowing electricity when the sun isn't shining or the wind isn't blowing allows the use of the stored energy, such as in a fuel cell that runs on hydrogen.
Electrons are often stored in batteries, but Bullock and his colleagues want to take advantage of the closer packing available in chemicals.
"We want to store energy as densely as possible. Chemical bonds can store a huge amount of energy in a small amount of physical space," said Bullock, director of the Center for Molecular Electrocatalysis at PNNL, one of DOE's Energy Frontier Research Centers. The team also included visiting researcher Monte Helm from Fort Lewis College in Durango, Colo.
Biology stores energy densely all the time. Plants use photosynthesis to store the sun's energy in chemical bonds, which people use when they eat food. And a common microbe stores energy in the bonds of hydrogen gas with the help of a protein called a hydrogenase.
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.
Two Plus Two Equals One
In this study, the researchers looked at only one small part of splitting water into hydrogen gas, like fast-forwarding to the end of a movie. Of the many steps, there's a part at the end when the catalyst has a hold of two hydrogen atoms that it has stolen from water and snaps the two together.
The catalyst does this by completely dismantling some hydrogen atoms from a source such as water and moving the pieces around. Due to the simplicity of hydrogen atoms, those pieces are positively charged protons and negatively charged electrons. The catalyst arranges those pieces into just the right position so they can be put together correctly. "Two protons plus two electrons equals one molecule of hydrogen gas," says Bullock.
