Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 1 of 1
Full-Text Articles in Life Sciences
Coordination Of Peroxide To The Cum Center Of Peptidylglycine Α-Hydroxylating Monooxygenase (Phm): Structural And Computational Study, Betty A. Eipper, Richard E. Mains
Coordination Of Peroxide To The Cum Center Of Peptidylglycine Α-Hydroxylating Monooxygenase (Phm): Structural And Computational Study, Betty A. Eipper, Richard E. Mains
UCHC Articles - Research
Many bioactive peptides, such as hormones and neuropeptides, require amidation at the C terminus for their full biological activity. Peptidylglycine α-hydroxylating monooxygenase (PHM) performs the first step of the amidation reaction—the hydroxylation of peptidylglycine substrates at the Cα position of the terminal glycine. The hydroxylation reaction is copper- and O2-dependent and requires 2 equiv of exogenous reductant. The proposed mechanism suggests that O2 is reduced by two electrons, each provided by one of two nonequivalent copper sites in PHM (CuH and CuM). The characteristics of the reduced oxygen species in the PHM reaction and …