It wasn’t all that long ago that I shared the news of Australia’s recent push toward hydrogen power. Bringing this conversation stateside, researchers from the University of Illinois Champaign-Urbana and the University of California Davis recently published a new study looking for a more efficient method for generating hydrogen gas.
According to reporting on ScienceDaily.com, the current production process for hydrogen gas is complex and hinders this alternative fuel industry from proliferating. As a result, researchers have invested in biologically synthesized hydrogen as a more efficient method of production.
In this latest study, researchers looked at iron-iron hydrogenases, or biological enzymes, because they’re known to be more rapid, ScienceDaily reports. To begin, they hypothesized that 10 parts made up the active sites within the enzyme. These parts included four carbon monoxide molecules, two cyanide ions, two iron ions and two groups of cysteine, a sulfur-containing amino acid.
As the study continued, they found that while there were likely still 10 parts, it was more likely that the sites were made up of two groups tightly bonded, and these identical groups contained two carbon monoxide molecules, one cyanide ion, one iron ion and one cysteine group.
However, they found their assumptions were wrong again. Thomas Rauchfuss, chemistry professor and study co-author, explains, “Our recipe is incomplete. We now know that 11 bits are required to make the active site engine, not 10, and we are on the hunt for that one final bit.”
While they haven’t found that final key element yet, the researchers say that the new understanding could lead to a more efficient means of producing hydrogen gas, thus clearing the way for the hydrogen fuel industry.
On another note, they say that this study could provide an assembly kit for other catalyst design project. “The take-away from this study is that it is one thing to envision using the real enzyme to product hydrogen gas, but it is far more powerful to understand its makeup well enough to be able to reproduce it for use in the lab,” Rauchfuss said.
