Abstract
Ascorbate was not required for the binding of 2-oxoglutarate to pure prolyl hydroxylase, and the enzyme catalyzed hydroxylation in the absence of ascorbate at an essentially maximal rate for 5–10 s, corresponding to 15–30 reaction cycles. After about one min the reaction rate in the absence of ascorbate was very low, even though only 1–2 % of the free bivalent iron had become oxidized. These and additional data indicate that prolyl hydroxylase can catalyze a number of reaction cycles without ascorbate, but at some stage the hydroxylation ceases, probably due to oxidation of the enzyme-bound iron, and ascorbate is then required as a quite specific reductant to re-activate the enzyme.
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