Renowned physicist Richard Feynman once said that biology can be explained by understanding the “wiggling and jiggling” of atoms. For the first time, a research team led by the University of Bristol is describing how this movement of atoms is strategically choreographed within enzymes to enable organisms to live at different temperatures.
Enzymes are the proteins that act as catalysts to make biological reactions happen. This is the first study to link the subtle dance of an enzyme to its ideal temperature.
The findings of the study also suggest that proteins successfully evolved as catalysts because of their ability to control their own movement in response to chemical reactions.
Dr. Marc van der Kamp and colleagues observed that the heat capacity of enzymes changes during catalytic activity. They found that the extent of this change is the critical factor in determining the temperature at which the enzyme works best.
“Our computer simulations of the ‘wiggling and jiggling’ of enzymes at different stages in the reaction tells us how these structural fluctuations give rise to the difference in heat capacity, and thereby can predict the optimum temperature of an enzyme,” said Dr. Van der Kamp. “Our work demonstrated that we can do this accurately for two completely different enzymes, by comparing to experimental data.”
“What is fascinating to see is that the whole enzyme structure is important: the ‘dance’ does not only change close to where the chemical reaction takes place, but also in parts much further away. This has consequences for evolution: the combination of the enzyme structure and the reaction the enzyme catalyses will define its optimal working temperature. A subtle change in structure can change the ‘dance’.”
The research may provide new insights for the development of improved biocatalysts used in industrial processes, such as the production of drugs.
The study is published in Nature Communications.
By Chrissy Sexton, Earth.com Staff Writer
Image Credit: Dr Marc van der Kamp and Michael Connolly