Researchers "unmask" enzyme catalysis
22 Oct 2013
Research from the University of Bristol (UOB) is significantly advancing the understanding of how certain protein enzymes increase the rate of chemical reaction, according to one expert paper.
The researchers believe that understanding exactly how enzymes increase reaction rates - typically much more effectively and under more environmentally friendly conditions than artificial catalysts - is an important goal in biotechnology development.
Our work shows that enzyme motions are involved in the reaction through a passive rather than an active mechanism
Professor Adrian Mulholland
Therefore, a thorough understanding of how enzymes achieve their rate enhancements is of great importance to fields like biocatalysis, bioenergy, drug design and the emerging field of synthetic biology.
Some recent theories have proposed that internal “promoting motions” of the enzyme are used to drive the chemistry. However, this remains a topic of considerable debate among experts.
The team, which included Dr David Glowacki, Professor Jeremy Harvey and Professor Adrian Mulholland from Bristol’s School of Chemistry, were able to alter the enzyme’s motions on a wide range of timescales whilst leaving its chemical properties unchanged.
The researchers found no significant role for “promoting motions” in the reaction, but did demonstrate a general coupling of enzyme motions to the catalysed reaction.
Professor Mulholland said: “Our work shows that enzyme motions are involved in the reaction through a passive rather than an active mechanism, and ultimately indicates that enzymes are not fundamentally different from man-made catalysts, they are just much better.
“This is an important thing to establish as knowing how enzymes work has far-reaching implications, for example in biotechnology and synthetic biology, and should help in the design of effective ’green’ catalysts in the future,” Mulholland added.
The work has been published in Proceedings of the National Academy of Sciences (PNAS).
