>
Fly British Flags In UK And Face Jail... But Pakistan And Palestine Flags Get A Pass
CIA Director Pushed Trump-Putin-Zelensky Summit During Moscow Visit: Report
Iceland Voters Reject Reopening Talks To Join European Union
"Profound Game-Changer": Musk Launching New Turbine Blade Factory To Solve Shortage...
Here's What to Expect as Air Taxis Actually Begin to Take Off
'Wood Foam' Startup Uses Logging Waste as Substitute for Plastic, Producing 400 Pounds Daily
How a Group of Young Men in 1933 Solved a Water Crisis in The Desert -- And Nobody Knows About It
This American Battery Could Break China's Grip On The EV Supply Chain
Tesla's Cybercab Launch Is Next Week. Here's What Tesla Still Needs To Prove
800-passenger commercial plane boldly reinvents how we will fly
Does Ultra-Fast Charging Ruin An EV Battery? BYD Did It 350 Times In 9 Days To Find Out
Singapore is experimenting with biological computing using living human neurons...
It's Happening - Europe is Building an Impossible Fusion Reactor
Portable 1MW Kaleidos Microreactor Secures Critical Nuclear Fuel Deal Through 2030s

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.