The University of Manchester team, working with colleagues in Bristol, has provided a unique insight into the working of enzymes ?biological molecules that speed up chemical reactions in the body.
When these chemical reactions go wrong they can lead to disease, so modern drugs are designed to target enzymes and 'switch them off'.
But their ability to accelerate chemical reactions means enzymes are also used in a number of commercial processes, including brewing, food processing, domestic cleaning and paper manufacturing.
"Improving our fundamental knowledge of how enzymes work is important to a wide range of pharmaceutical and industrial fields," said Professor Nigel Scrutton, one of the lead researchers at Manchester.
"Enzymes are central to the existence of life because most chemical reactions in our cells would take place too slowly or produce a different outcome without their involvement.
"But when enzymes malfunction they can cause serious diseases, so modern drugs are designed to prevent enzymes accelerating, or 'catalysing', inappropriate reactions.
"Our research has shown at an atomic level how enzymes act as catalysts; the findings are a radical departure from the traditional view of how they work and might explain why attempts to make artificial enzymes have so far been disappointing.
The work ?published as a major research article in the leading journal Science ?builds on earlier studies by Professor Scrutton and Manchester colleagues, Professor Michael Sutcliffe and Dr David Leys.
Together they have shown, now in unprecedented detail, how enzymes avoid unfavourable energy barriers caused by the resistance to a reaction by allowing matter to 'flow through' the barrier ?a process known as quantum mechanical tunnelling.
Source:University of Manchester