That's the idea. Getting there will require a team of Berkeley Lab scientists and industrial partners.
John Tainer's and Steve Yannone's groups in Berkeley Lab's Life Sciences Division will explore how the enzyme can be tweaked so that it binds with methane. They'll use computational analysis to map the structural changes needed so that the enzyme has a shot at breaking methane's bonds and snaring the molecule. They'll also study the enzyme at Berkeley Lab's Advanced Light Source, where the SIBYLS synchrotron beamline combines X-ray scattering with X-ray diffraction capabilities. This will help the scientists determine the enzyme's functional 3-D structure.
In addition, Novici Biotech, a California-based industrial partner, will create tens of thousands of variants of the enzyme with its proprietary synthetic biology technology. Romy Chakraborty of Berkeley Lab's Earth Sciences Division and scientists from the U.S. Department of Energy's Joint BioEnergy Institute will assist in analyzing these variants to identify those with the best characteristics.
Ideally, each step will circle closer to a new enzyme that's very efficient at converting methane to an oxidized product.
"Once a functional methylase has been constructed, we need to engineer a new metabolic cycle that takes up methane and regenerates the co-substrate," says Jansson. "Just like the Calvin-Benson cycle, but with assimilation of methane instead of carbon dioxide."
"This will take some time," Jansson says. "But if we're successful, the methylase can be installed into various microorganisms such as E. coli, yeast, and cyanobacteria and used on a large s
|Contact: Dan Krotz|
DOE/Lawrence Berkeley National Laboratory