Reactions of 1,10‐phenanthroline (phen) and 2‐(3,4‐dichlorophenyl)acetic acid (dcaH) with
Mn(CO
3) (
M = Li
I, Na
I and Mg
II;
n = 1 and 2) in MeOH yield the mononuclear lithium complex aqua[2‐(3,4‐dichlorophenyl)acetato‐κ
O](1,10‐phenanthroline‐κ
2N,
N′)lithium(I), [Li(C
8H
5Cl
2O
2)(C
12H
8N
2)(H
2O)] or [Li(dca)(phen)(H
2O)] ( 1 ), the dinuclear sodium complex di‐μ‐aqua‐bis{[2‐(3,4‐dichlorophenyl)acetato‐κ
O](1,10‐phenanthroline‐κ
2N,
N′)sodium(I)}, [Na
2(C
8H
5Cl
2O
2)
2(C
12H
8N
2)
2(H
2O)
2] or [Na
2(dca)
2(phen)
2(H
2O)
2] ( 2 ), and the one‐dimensional chain magnesium complex
catena‐poly[[[diaqua(1,10‐phenanthroline‐κ
2N,
N′)magnesium]‐μ‐2‐(3,4‐dichlorophenyl)acetato‐κ
2O:
O′] 2‐(3,4‐dichlorophenyl)acetate monohydrate], {[Mg(C
8H
5Cl
2O
2)(C
12H
8N
2)(H
2O)
2](C
8H
5Cl
2O
2)·H
2O}
n or {[Mg(dca)(phen)(H
2O)
2](dca)·H
2O}
n ( 3 ). In these complexes, phen binds
via an
N,
N′‐chelate pocket, while the deprotonated dca
? ligands coordinate either in a monodentate (in 1 and 2 ) or bidentate (in 3 ) fashion. The remaining coordination sites around the metal ions are occupied by water molecules in all three complexes. Complex 1 crystallizes in the triclinic space group
P with one molecule in the asymmetric unit. The Li
+ ion adopts a four‐coordinated distorted seesaw geometry comprising an [N
2O
2] donor set. Complex 2 crystallizes in the triclinic space group
P with half a molecule in the asymmetric unit, in which the Na
+ ion adopts a five‐coordinated distorted spherical square‐pyramidal geometry, with an [N
2O
3] donor set. Complex 3 crystallizes in the orthorhombic space group
P2
12
12
1, with one Mg
2+ ion, one phen ligand, two dca
? ligands and three water molecules in the asymmetric unit. Both dcaH ligands are deprotonated, however, one dca
? anion is not coordinated, whereas the second dca
? anion coordinates in a bidentate fashion bridging two Mg
2+ ions, resulting in a one‐dimensional chain structure for 3 . The Mg
2+ ion adopts a distorted octahedral geometry, with an [N
2O
4] donor set. Complexes 1 – 3 were evaluated against urease and α‐glucosidase enzymes for their inhibition potential and were found to be inactive.
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