>
You Only Had To Listen: Ron Paul Destroys Mike Johnson For Betraying America
Watch: Migrants Gone Wild On Streets Of Midtown Manhattan
How to Defeat A Gatekeeper – #SolutionsWatch
Blazing bits transmitted 4.5 million times faster than broadband
Scientists Close To Controlling All Genetic Material On Earth
Doodle to reality: World's 1st nuclear fusion-powered electric propulsion drive
Phase-change concrete melts snow and ice without salt or shovels
You Won't Want To Miss THIS During The Total Solar Eclipse (3D Eclipse Timeline And Viewing Tips
China Room Temperature Superconductor Researcher Had Experiments to Refute Critics
5 video games we wanna smell, now that it's kinda possible with GameScent
Unpowered cargo gliders on tow ropes promise 65% cheaper air freight
Wyoming A Finalist For Factory To Build Portable Micro-Nuclear Plants
Yet we know very little about how the complex reaction occurs, limiting our ability to use the double benefit to our advantage.
By studying the enzyme the bacteria use to catalyze the reaction, a team at Northwestern University now has discovered key structures that may drive the process.
Their findings ultimately could lead to the development of human-made biological catalysts that convert methane gas into methanol.
"Methane has a very strong bond, so it's pretty remarkable there's an enzyme that can do this," said Northwestern's Amy Rosenzweig, senior author of the paper. "If we don't understand exactly how the enzyme performs this difficult chemistry, we're not going to be able to engineer and optimize it for biotechnological applications."
The enzyme, called particulate methane monooxygenase (pMMO), is a particularly difficult protein to study because it's embedded in the cell membrane of the bacteria.