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- Title
Thioether‐Containing Copper Complexes as PHM, DβM, and TβM Model Systems.
- Authors
Gómez‐Vidales, Virginia; Castillo, Ivan
- Abstract
This minireview presents efforts of synthetic chemists to mimic the active site of the copper monooxygenase enzymes peptidylglycine α‐hydroxylating monooxygenase (PHM), dopamine β‐monooxygenase (DβM), and tyramine β‐monooxygenase (TβM), all of which feature copper‐thioether ligation in their resting states. These monooxygenases are involved in the initial activation of O2 to generate neurotransmitters by the selective activation of C−H bonds of their corresponding substrates, resulting in subsequent hydroxylation. Attempts to emulate the N2S donor set provided by the two histidines and the methionine residues that coordinate to copper in the active site employ N2S and N3S‐type ligands, with the latter ones providing the best conditions for testing the reactivity of their CuI complexes with dioxygen. Identification of CuII‐superoxos as capable agents for C−H activation has provided support for these species as the key reactive intermediates in the enzymatic systems. Synthetic end‐on [CuII‐η1‐O2.−] and side‐on [CuII‐η2‐O2.−] cupric superoxos are capable of such transformations, which is related to the open question of whether the methionine S‐donor may act as a hemilabile ligand in biological systems.
- Subjects
COPPER enzymes; COPPER compounds; BIOLOGICAL systems; MONOOXYGENASES; CHEMISTS; LIGANDS (Chemistry); DOPAMINE receptors
- Publication
European Journal of Inorganic Chemistry, 2022, Vol 2022, Issue 1, p1
- ISSN
1434-1948
- Publication type
Article
- DOI
10.1002/ejic.202100728