Journal article

Publication year: 2013

Pages: 1504-1511

Journal: Journal of Inorganic and General Chemistry

Volume number: 639

Issue number: 8-9

ISSN: 0044-2313

DOI Link: https://doi.org/10.1002/zaac.201300066

Publisher: Wiley

Abstract: 
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.

Harvard Citation style: Hoppe, T., Josephs, P., Kempf, N., Wolper, C., Schindler, S., Neuba, A., et al. (2013) An Approach to Model the Active Site of Peptidglycine-alpha-hydroxylating monooxygenase (PHM), Zeitschrift für anorganische und allgemeine Chemie = Journal of Inorganic and General Chemistry, 639(8-9), pp. 1504-1511. https://doi.org/10.1002/zaac.201300066

APA Citation style: Hoppe, T., Josephs, P., Kempf, N., Wolper, C., Schindler, S., Neuba, A., & Henkel, G. (2013). An Approach to Model the Active Site of Peptidglycine-alpha-hydroxylating monooxygenase (PHM). Zeitschrift für anorganische und allgemeine Chemie = Journal of Inorganic and General Chemistry. 639(8-9), 1504-1511. https://doi.org/10.1002/zaac.201300066