Rational Design of a Histidine–Methionine Site Modeling the M‑Center of Copper Monooxygenases in a Small Metallochaperone Scaffold

Mononuclear copper monooxygenases peptidylglycine monooxygenase (PHM) and dopamine β-monooxygenase (DBM) catalyze the hydroxylation of high energy C–H bonds utilizing a pair of chemically distinct copper sites (CuH and CuM) separated by 11 Å. In earlier work, we constructed single-site PHM variants...

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Veröffentlicht in:	Biochemistry (Easton) 2019-07, Vol.58 (28), p.3097-3108
Hauptverfasser:	Alwan, Katherine B, Welch, Evan F, Arias, Renee J, Gambill, Ben F, Blackburn, Ninian J
Format:	Artikel
Sprache:	eng
Schlagworte:	active sites Animals azides Binding Sites - physiology catalytic activity chemical bonding copper Copper - chemistry Copper - metabolism dopamine dopamine beta-monooxygenase energy Histidine - chemistry Histidine - metabolism hydroxylation ligands Metallochaperones - chemistry Metallochaperones - metabolism methionine Methionine - chemistry Methionine - metabolism Mixed Function Oxygenases - chemistry Mixed Function Oxygenases - metabolism Models, Chemical oxygen Protein Structure, Secondary reducing agents site-directed mutagenesis spectral analysis
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