The study of how molecular machines assemble and maintain our bodies is one of the defining sciences of our generation. The more we learn about these machines, the more complex and capable they seem.
One feature common to all machines is that they work best within a certain temperature range. Many human-built machines have complex systems for maintaining their temperature. Similarly, many machines built by evolution have extremely efficient thermal management systems. Think big ears and sweat glands.
So it seems reasonable to assume that evolution might have found a
way for molecular machines to manage their temperature.
Today, Hans Briegel at the University of Innsbruck in Austria and Sandu Popescu at the University of Bristol in the UK, put forward a fascinating suggestion for how such a thermal management system might work.
The machines they focus on are enzymes, machines which catalyse
certain biochemical reactions.
Essentially, enzymes are molecular clamps. They grab hold of specific biomolecules and hold them still. This reduces the activation energy of whatever chemical process the biomolecules are involved in, thereby increasing the reaction rate.
But the performance of enzymes is extremely sensitive to temperature. The rate of the reactions they catalyse increases slowly with temperature until it reaches a maximum and then drops dramatically.
On a mechanical level, the extra heat increases the amount of vibration in the molecular structure of the machine. The specific problem for an enzyme is the vibrations in the set of “molecular jaws” it uses to grab hold of biomolecules (otherwise called the activation site).
As the temperature increases, the vibrations in these jaws increases until they are no longer able to grab the biomolecules they are designed to hold. That’s when the reaction rate drops dramatically.
Briegel and Popescu say that it would be hugely advantageous for an enzyme to be able to cool these jaws. And they map out one way this could be done, which they call conformational cooling.
The idea is that a small change in the enzyme’s shape stiffens the jaws temporarily. This has the effect of reducing the vibrations in the jaws and hence their temperature. When the cooled jaws relax, they are then able to grab hold of the relevant biomolecules again. At least until they heat up again.
(The key is that the jaws must relax faster than the rate at which they heat up, otherwise there’s no advantage.)
Of course, every refrigerator needs a source of power and Briegel and Popescu suggest that this could be provided by another molecule, such as ATP.
What’s neat about this suggestion is that a very simple experiment could easily test it. Simply measure the temperature dependency of the rate of enzymatic reaction with and without the presence of ATP.
If ATP is really providing the energy to cool the enzyme, then the two curves should be different.
That’s an experiment that an enterprising grad student could do tomorrow.
Let us know how you get on.
Ref: arxiv.org/abs/0912.2365: Intra-Molecular Refrigeration in Enzymes