Reaction mechanism of the bicopper enzyme peptidylglycine α-hydroxylating monooxygenase.

ABSTRACT: Peptidylglycine α-hydroxylating monooxygenase is a noninteracting bicopper enzyme that stereospecifically hydroxylates the terminal glycine of small peptides for its later amidation. Neuroendocrine messengers, such as oxytocin, rely on the biological activity of this enzyme. Each catalytic turnover requires one oxygen molecule, two protons from the solvent, and two electrons. Despite this enzyme having been widely studied, a consensus on the reaction mechanism has not yet been found. Experiments and theoretical studies favor a pro-S abstraction of a hydrogen atom followed by the rebinding of an OH group. However, several hydrogen-abstracting species have been postulated; because two protons are consumed during the reaction, several protonation states are available. An electron transfer bet

SUBMITTER: Abad E 

PROVIDER: S-EPMC4022847 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature