Illinois scientists closing in on renewable energy source

Original source:
http://www.sciencedaily.com/releases/2005/10/051006082610.htm

Summary:

• Researchers at the Beckman Institute for Advanced Science and Technology at the University of Illinois at Urbana-Champaign have opened a window by way of computer simulation that lets them see how and where hydrogen and oxygen travel to reach and exit an enzyme's catalyst site -- the H cluster -- where the hydrogen is converted into energy.
• The Illinois scientists and three colleagues from the National Renewable Energy Laboratory in Golden, Colo., detailed their findings in the September issue of the journal Structure.
• What they found could help solve a long-standing economics problem.
• Because oxygen permanently binds to hydrogen in the H cluster, the production of hydrogen gas is halted.
• "Understanding how oxygen reaches the active site will provide insight into how hydrogenase's oxygen tolerance can be increased through protein engineering, and, in turn, make hydrogenase an economical source of hydrogen fuel," said Klaus Schulten, Swanlund Professor of Physics at Illinois and leader of the Beckman's Theoretical Biophysics Group.
• Using computer modeling developed in Schulten's lab -- Nanoscale Molecular Dynamics (NAMD) and Visual Molecular Dynamics (VMD) -- physics doctoral student Jordi Cohen created an all-atom simulation model based on the crystal structure of hydrogenase CpI from Clostridium pasteurianum.
• This model allowed Cohen to visualize and track how oxygen and hydrogen travel to the hydrogenase's catalytic site, where the gases bind, and what routes the molecules take as they exit.
• Using a new computing concept, he was able to describe gas diffusion through the protein and predict accurately the diffusion paths typically taken.
• Because the protein is more porous to hydrogen than to oxygen, the hydrogen diffused through the oxygen pathways but also through entirely new pathways closed to oxygen, the researchers discovered.

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