36489-03-9Relevant articles and documents
An approach to model the active site of peptidglycine-α-hydroxylating monooxygenase (PHM)
Hoppe, Tobias,Josephs, Patrick,Kempf, Natascha,Woelper, Christoph,Schindler, Siegfried,Neuba, Adam,Henkel, Gerald
, p. 1504 - 1511 (2013)
The copper(I) and copper(II) complexes [Cu((TMGet) 2NetSEt)]BPh4 (1·BPh4) and [Cu((TMGet)2NetSEt)Cl]Cl (2·Cl) with (TMGet)2NetSEt = ((Me2N) 2C=NCH2CH2)2NCH2CH 2SEt 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·BPh4 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. Copyright