Abstract
At the conclusion of the Royal Society discussion on lysozyme a little over two years ago, I had to follow Monod and elevate myoglobin and haemoglobin to the rank of honorary enzymes so as to draw my generalizations from three structures rather than a single one. I then suggested that the powerful catalytic activity of enzymes was due to the medium of low dielectric constant provided by their non-polar interior, which allowed strong electrical interactions to take place between the active site and the substrate. The structures of the six additional enzymes which have since been solved have confirmed this view, but they have also shown that it should be broadened. It appears that in the medium of low dielectric constant a free charge introduces a large free energy. To regain stability two alternative devices are open to the enzyme: (1) to compensate the charge internally; (2) to design a system of bonds which transfers the charge to the surface.

This publication has 0 references indexed in Scilit: