Abstract
An inspection of the active site region of metallo-enzymes leads to two conclusions. (i) Individual attacking groups usually have uncommon physical properties, (ii) The active site region is cooperatively linked with a large part of the enzyme. Such an interaction is common to heterogeneous catalysts but is absent in homogeneous catalysts. It is concluded that the energetics of catalysis requires an analysis of the nature of cooperativity in microdomains of well organized material and some general remarks as to the problems which arise are described. Methods of examining large well-organized molecules (microdomains) are described and some suggestions are made as to how man-made ‘enzymes’ could be produced.
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