An Approach to Model the Active Site of Peptidglycine-alpha-hydroxylating monooxygenase (PHM)

作者：Hoppe Tobias; Josephs Patrick; Kempf Natascha; Woelper Christoph; Schindler Siegfried^*; Neuba Adam; Henkel Gerald

来源：Zeitschrift fur Anorganische und Allgemeine Chemie, 2013, 639(8-9): 1504-1511.

DOI：10.1002/zaac.201300066

• Copper
• Dioxygen activation
• Model compounds
• Guanidine ligands
• Crystal structure

The copper(I) and copper(II) complexes [Cu((TMG(et))(2)-NetSEt)]BPh4 (1 center dot BPh4) and [Cu((TMG(et))(2)NetSEt)Cl]Cl (2 center dot Cl) with (TMG(et))(2)NetSEt = ((Me2N)(2)C=NCH2CH2)(2)NCH2CH2SEt 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 center dot 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-mu-oxo and a side-on peroxide complex was detected spectroscopically.

• 出版日期2013-7