Skip to Main Content U.S. Department of Energy
Science Directorate
Page 620 of 1002

Physcial Sciences Division
Research Highlights

August 2011

Catalyst That Makes Hydrogen Gas Breaks Speed Record

Material designed for energy applications is10 times faster than natural enzyme, uses inexpensive metals

Hydrogen Catalyst
The record-breaking catalyst stuffs electrons - the backbone of electricity, seen here as yellow balls or yellow halos - into chemical bonds between hydrogen atoms (H) stolen from water. It uses inexpensive nickel (Ni) to do so, instead of the more common and expensive platinum. Enlarge Image

Results: Looking to nature for their muse, researchers at Pacific Northwest National Laboratory 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.

Why It Matters: This reaction 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 highly active 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 very expensive metals such as platinum.

"This nickel-based catalyst is really very fast," said coauthor Dr. Morris Bullock, Director of the Center for Molecular Electrocatalysis at PNNL. "It's about a hundred times faster than the previous molecular catalyst record holder. And from nature, we knew it could be done with abundant and inexpensive nickel or iron."

To learn more, read the press release.

Also, you can now view the abstract, reprint, and full text of the article in Science directly, without having to go through the Science member login screen.

Acknowledgments: This work was supported by the U.S. Department of Energy Office of Science.

This work was done by Monte L. Helm, visiting researcher from Fort Lewis College; Michael P. Stewart, R. Morris Bullock, M. Rakowski DuBois, Daniel L. DuBois of PNNL.

Reference: Monte L. Helm, Michael P. Stewart, R. Morris Bullock, M. Rakowski DuBois, Daniel L. DuBois, "A Synthetic Nickel Electrocatalyst With a Turnover Frequency Above 100,000 s-1 for H2 Production." Science 333(6044):863-866. DOI 10.1126/science.1205864.


Page 620 of 1002

Science at PNNL

Core Research Areas

User Facilities

Centers & Institutes

Additional Information

Research Highlights Home

Share

Print this page (?)

YouTube Facebook Flickr TwitThis LinkedIn

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.

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, the researchers wanted to pull out the active portion of the biological hydrogenase and redesign it with a stable chemical backbone.

Contacts