The fate of the energy released during the formation of the enzyme-sub
strate complexes is discussed in connection with energetic aspects of
the one-substrate enzyme-catalysed reaction. Assuming a free and rapid
intramolecular energy flow in the complex, the high enzyme catalytic
activity cannot be explained. it is suggested that a metal ion near th
e active site can serve as a barrier to the energy flow from the bindi
ng sites of the complex into the enzyme molecule. The effective vibrat
ional temperature of the bonded substrate molecule is then higher than
the temperature of the reaction system. (C) 1995 Academic Press Limit
ed