Heterogeneous catalyst goes enzymatic

phys.org | 1/24/2019 | Staff
amyc9948amyc9948 (Posted by) Level 3
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What if there were no tunnels in the Swiss Alps? Anyone trying to travel through them would have to go up and down hills and zigzag around the ranges. A lot more energy and time is saved by passing through a tunnel than climbing a mountain. This is similar to how catalysts work: they speed up chemical reactions by lowering the energy required to reach the desired physical state.

In industrial manufacturing processes, heterogeneous catalysis, which typically involves the use of solid catalysts placed in a liquid or gas reaction mixture, has many potential applications. Being in a different phase, heterogeneous catalysts can be easily separated from a reaction mixture. In this way, the catalysts can be effectively recovered and recycled, being quite eco-friendly. In addition, they exhibit very stable activity even under harsh reaction conditions. Despite such advantages, heterogeneous catalysis has been thought to allow for less interaction and controllability than homogeneous catalysis due to a poor understanding of its reaction process.

Researchers - Center - Nanoparticle - Research - Director

Researchers at the Center for Nanoparticle Research (led by Director Taeghwan Hyeon) within the Institute for Basic Science (IBS) in collaboration with Professor Ki Tae Nam at Seoul National University and Professor Hyungjun Kim at KAIST demonstrated enzyme-like heterogeneous catalysis for the first time. They developed a highly active heterogeneous TiO2 photocatalyst incorporated with many single copper atoms. They used this catalyst for photocatalytic hydrogen production, and found that the catalyst is as active as the most active and expensive Pt-TiO2 catalyst.

The researchers were committed to modeling the catalyst structure in a similar way to the most efficient and reactive catalysts that are biological enzymes. Enzymes comprise catalytically active metal atoms and surrounding proteins that work very closely to keep their feedbacks moving back and forth. Thanks to this cooperative internal communication, enzymes can swiftly adapt their structure to...
(Excerpt) Read more at: phys.org
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