Pub. Date : 2006 Dec
PMID : 17019721
4 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Copper-oxygen complexes supported by beta-diketiminate and anilido-imine ligands have recently been reported (Aboelella et al., J Am Chem Soc 2004, 126, 16896; Reynolds et al., Inorg Chem 2005, 44, 6989) as potential biomimetic models for dopamine beta-monooxygenase (DbetaM) and peptidylglycine alpha-hydroxylating monooxygenase (PHM). | Oxygen | peptidylglycine alpha-amidating monooxygenase | Homo sapiens |
| 2 | Copper-oxygen complexes supported by beta-diketiminate and anilido-imine ligands have recently been reported (Aboelella et al., J Am Chem Soc 2004, 126, 16896; Reynolds et al., Inorg Chem 2005, 44, 6989) as potential biomimetic models for dopamine beta-monooxygenase (DbetaM) and peptidylglycine alpha-hydroxylating monooxygenase (PHM). | Oxygen | peptidylglycine alpha-amidating monooxygenase | Homo sapiens |
| 3 | Based on these results, design strategies for new DbetaM and PHM biomimetic ligands are proposed: new ligands should be made less electron rich so as to favor end-on dioxygen coordination in the 1:1 Cu-O(2) adducts. | Oxygen | peptidylglycine alpha-amidating monooxygenase | Homo sapiens |
| 4 | Comparison of the relative reactivities of the various copper-oxygen complexes as hydroxylating agents provides support for a Cu(II)-superoxide species as the intermediate responsible for substrate hydroxylation in DbetaM and PHM, and suggests that a Cu(III)-oxo intermediate would be competent in this process as well. | Oxygen | peptidylglycine alpha-amidating monooxygenase | Homo sapiens |