The research, published in the journal Nature, reveals a new mechanism by which enzymes can control chemical reactions. This mechanism, called "conformational selection," involves the enzyme changing its shape in order to bind to a substrate molecule and catalyze a reaction.
"This is a major breakthrough in our understanding of how enzymes work," said study lead author Dr. Andrei Tokmakoff, professor of chemistry in the UB College of Arts and Sciences. "For decades, scientists have believed that enzymes work by lowering the activation energy of a reaction, but our research shows that conformational selection is also a critical factor."
Activation energy is the energy required to start a chemical reaction. By lowering the activation energy, enzymes can speed up reactions that would otherwise be too slow to occur at room temperature.
Conformational selection, on the other hand, involves the enzyme changing its shape in order to bind to a substrate molecule. This change in shape creates a specific environment that allows the enzyme to catalyze a reaction.
"The discovery of conformational selection as a mechanism of enzyme catalysis has important implications for the development of new drugs and treatments," said Tokmakoff. "By understanding how enzymes work, we can design drugs that can inhibit or activate specific enzymes, which could lead to new treatments for a variety of diseases."
The research team used a variety of techniques, including X-ray crystallography, nuclear magnetic resonance spectroscopy, and molecular dynamics simulations, to study the mechanism of conformational selection in enzymes.
The findings of the study provide a new framework for understanding how enzymes work and could lead to the development of new drugs and treatments for a variety of diseases.
In addition to Tokmakoff, the research team included Dr. Alexander Mozzhukhin, a former postdoctoral researcher in Tokmakoff's lab, and Dr. Yifan Song, a current postdoctoral researcher in the lab.
