An Approach to Model the Active Site of Peptidglycine‐α‐hydroxylating monooxygenase (PHM)

The copper(I) and copper(II) complexes [Cu((TMG et ) 2 N et SEt)]BPh 4 ( 1· BPh 4 ) and [Cu((TMG et ) 2 N et SEt)Cl]Cl ( 2· Cl) with (TMG et ) 2 N et SEt = ((Me 2 N) 2 C=NCH 2 CH 2 ) 2 NCH 2 CH 2 SEt were synthesized and structurally characterized as a model system for the copper enzyme PHM, a monooxygenase involved in the activation of peptide hormones and neuropeptides. The reaction of the copper(I) complex 1· BPh 4 with dioxygen has been studied using low temperature stopped‐flow methods. However, in contrast to PHM no formation of an end‐on copper superoxido complex could be observed. Instead an equilibrium between a bis‐μ‐oxo and a side‐on peroxide complex was detected spectroscopically.