Night of the living enzyme( that varied depending on the enzyme to...)

Picture an enzyme in solution, floating unfolded like a mop head suspended in a water bucket. When that enzyme comes into contact with a pore, the protein is pulled into place by the oppositely charged FMS and squeezed into active shape inside the pore. So loaded, the pore is now open for business; substances in the solution that come into contact with the enzyme can now be catalyzed into the desired product. For example, GI turns glucose to fructose, and standard tests for enzyme activity confirmed that FMS-GI was as potent or better at making fructose as enzyme in solution. OPH activity doubled, while GOX activity varied from 30 percent to 160 percent, suggesting that the enzymes orientation in the pore is important.

It could be that in some cases the active site, the part of the enzyme that needs to be in contact with the chemical to be converted, was pointing the wrong way and pressed tightly against the walls of the pore, Ackerman said.

To show that the enzymes were trapped inside the FMS pores, the team stained the protein-FMS complex with gold nanoparticles and documented the enzyme-in-pore complex through electron microscopy. A spectroscopic analysis of the proteins squeezed into their active conformation turned up no new folds, evidence that they had neatly refolded rather than been forcibly wadded into the pore.

Ackerman said that this new understanding combined with new cell-free techniquesmaking hundreds of designer enzymes a day with components derived from cellswill speed the development of task-specific enzymes. This could lead to enzyme-based molecular machines in nanomaterials that carry out complex biological reactions to produce energy or remediate toxic pollutants.