Title : Effects of thioether substituents on the O2 reactivity of beta-diketiminate-Cu(I) complexes: probing the role of the methionine ligand in copper monooxygenases.

Pub. Date : 2006 Mar 15

PMID : 16522125






2 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 The activation of dioxygen by dopamine beta-monooxygenase (DbetaM) and peptidylglycine alpha-hydroxylating monooxygenase (PHM) is postulated to occur at a copper site ligated by two histidine imidazoles and a methionine thioether, which is unusual because such thioether ligation is not present in other O2-activating copper proteins. Oxygen peptidylglycine alpha-amidating monooxygenase Homo sapiens
2 The activation of dioxygen by dopamine beta-monooxygenase (DbetaM) and peptidylglycine alpha-hydroxylating monooxygenase (PHM) is postulated to occur at a copper site ligated by two histidine imidazoles and a methionine thioether, which is unusual because such thioether ligation is not present in other O2-activating copper proteins. Oxygen peptidylglycine alpha-amidating monooxygenase Homo sapiens