Stereochemical structure and biochemical activity of heme proteins

Abstract

A correlation between the stereochemical geometry around the metal ion in heme enzymes and their catalytic properties is attempted. It is shown that spin-lattice relaxation time measurement of bulk water in the enzyme solution gives accurate information as to the presence or absence of water molecule at the sixth coordination site of the heme iron. The rate of formation of compound I, an intermediate in the catalytic cycle of the enzymes, is shown to be directly related to the nature of the sixth coordination site of the heme.