The workings of an iron-laden bacterial enzyme could one day provide researchers with an inexpensive and stable catalyst to create hydrogen, according to scientists at Utah State University.
With funding from the National Science Foundation (NSF), biochemists John Peters and Lance Seefeldt have made a detailed description of the structure of an enzyme known as CpI, found in the soil microorganism Clostridium pasteurianum. The results of their research on the structure and function of CpI are published in the December 4 issue of the journal Science.
CpI is a hydrogenase, a type of enzyme used by microorganisms to make molecular hydrogen (H2), or through reversing the reaction, break down H2 into protons and electrons. Peters and Seefeldt's study suggests a mechanism by which CpI uses atoms of iron as a means to catalyze the production of H2.
"The iron-only hydrogenase is basically a means to get rid of unwanted electrons," said Kamal Shukla, NSF program manager. "Clostridium pasteurianum uses CpI to convert protons and electrons into (H2), a waste product."
What is a waste product to some organisms might be an incredibly useful product for others. According to Peters, a better understanding of this enzymatic process interests not only biologists and biochemists, but also researchers of alternative energy sources.
"Hydrogen is often mentioned as a future fuel source because it is a renewable and clean-burning energy carrier," said Peters. "The biological production of hydrogen, then, represents a tremendous reserve of energy that we may tap through our understanding of the mechanisms that have evolved in nature."
Attaining the three-dimensional structure of enzymes like CpI may be the
first step in tapping into that resource. Peters and Seefeldt depict CpI as a
collection of 20 iron atoms arranged in clusters around a mushroom shaped
framework. Electrons move in throug
Contact: Greg Lester
National Science Foundation