Abstract

Four superoxide dismutase active copper chelates, Cu(acetylsalicylate) 2, Cu(salicylate) 2, Cu(lysine) 2 and Cu(tyrosine) 2, proved to be inhibitors of prolyl and lysyl hydroxylase. The kinetics of the inhibition are consistent with the proposal that these compounds dismutated • O 2 staggered− at the active site of the enzymes. The data strongly suggest that • O 2 staggered− is the active form of O 2 in the prolyl and lysyl hydroxylase reactions.

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