Abstract
Recombination of apo horseradish peroxidase with 2,4 dimethyldeutero hemin and its mono- and dimethyl esters was performed. The number of free carboxyl side chains in these three hemins is 2, 1 and 0 respectively. Despite such a difference, all of these three reconstituted enzymes can react with H 2O 2 to produce compound I. The second order rate constants for compound I formation are 1.3 × 10 7 M −1s −1, 8.5 × 10 6 M −1s −1 and 5.9 × 10 6 M −1s −1. Therefore the propionate side chain of hemin has no direct role in compound I formation.
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