"What we discovered was surprising," Schulten said. "Both hydrogen and oxygen diffuse through the protein rather quickly, yet, there are clear differences."
Oxygen requires a bit more space compared with the lighter and smaller hydrogen, staying close to few well localized fluctuating channels. The hydrogen gas traveled more freely. 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.
The researchers concluded that it could be possible to close the oxygen pathways of hydrogenase through genetic modification of the protein and, thereby, increase the tolerance of hydrogenases to oxygen without disrupting the release of hydrogen gas.
Co-authors with Schulten and Cohen were Kwiseon Kim, Paul King and Michael Seibert, all of the National Renewable Energy Laboratory. The National Institutes of Health, National Science Foundation and the U.S. Department of Energy funded the research.
NAMD is a parallel molecular dynamics code designed for high-performance simulation of large biomolecular systems. VMD is a molecular visualization program for displaying, animating and analyzing large biomolecular systems using 3-D graphics.
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Contact: Jim Barlow, Life Sciences Editor
jebarlow@uiuc.edu
217-333-5802
University of Illinois at Urbana-Champaign
6-Oct-2005