An Approach to Model the Active Site of Peptidglycine‐α‐hydroxylating monooxygenase (PHM). Issue 8 (30th April 2013)

• Record Type: Journal Article
• Authors: Hoppe, Tobias; Josephs, Patrick; Kempf, Natascha; Wölper, Christoph; Schindler, Siegfried; Neuba, Adam; Henkel, Gerald
• Is Part Of: Zeitschrift für anorganische und allgemeine Chemie. Volume 639:Issue 8/9(2013)
• Page Start: 1504
• Page End: 1511
• Publication Date: 2013-04-30
• Subjects: Chemistry, Inorganic -- Periodicals; Chemistry -- Periodicals; 540
• DOI: 10.1002/zaac.201300066
• Languages: English
• ISSNs: 0044-2313

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>The copper(I) and copper(II) complexes [Cu((TMG_et)₂N_etSEt)]BPh₄ (<bold>1·</bold>BPh₄) and [Cu((TMG_et)₂N_etSEt)Cl]Cl (<bold>2·</bold>Cl) with (TMG_et)₂N_etSEt = ((Me₂N)₂C=NCH₂CH₂)₂NCH₂CH₂SEt 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 <bold>1·</bold>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.</p> </abstract>