How do copper enzymes hydroxylate aliphatic substrates? Recent insights from the chemistry of model systems.
Rolff
Malte
M
Institut für Anorganische Chemie, Christian Albrechts Universität Kiel, Otto Hahn Platz 6/7, 24098 Kiel, Germany.
Tuczek
Felix
F
D001665:Binding Sites; D003300:Copper / Q000737:chemistry / Q000378:metabolism*; D006900:Hydroxylation; D008024:Ligands; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000737:chemistry / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism*; D013379:Substrate Specificity
D008024:Ligands; D009097:Multienzyme Complexes; D003300:Copper; D006899:Mixed Function Oxygenases; C035189:peptidylglycine monooxygenase; D010100:Oxygen