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An Approach to Model the Active Site of Peptidglycine‐α‐hydroxylating monooxygenase (PHM)
Author(s) -
Hoppe Tobias,
Josephs Patrick,
Kempf Natascha,
Wölper Christoph,
Schindler Siegfried,
Neuba Adam,
Henkel Gerald
Publication year - 2013
Publication title -
zeitschrift für anorganische und allgemeine chemie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.354
H-Index - 66
eISSN - 1521-3749
pISSN - 0044-2313
DOI - 10.1002/zaac.201300066
Subject(s) - chemistry , copper , monooxygenase , active site , stereochemistry , enzyme , medicinal chemistry , organic chemistry , cytochrome p450
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.