ChemInform Abstract: Phosphate Anion Binding by Macrocyclic Dinucleating Ligands and Their Metal Complexes

ChemInform ◽  
2010 ◽  
Vol 31 (20) ◽  
pp. no-no
Author(s):  
Arthur E. Martell ◽  
Ramunas J. Motekaitis ◽  
Qin Lu ◽  
David A. Nation
Polyhedron ◽  
1999 ◽  
Vol 18 (25) ◽  
pp. 3203-3218 ◽  
Author(s):  
Arthur E. Martell ◽  
Ramunas J. Motekaitis ◽  
Qin Lu ◽  
David A. Nation

Heterocycles ◽  
2019 ◽  
Vol 98 (4) ◽  
pp. 551
Author(s):  
Quan Gan ◽  
Guoping Li ◽  
Jiulong Li ◽  
Chaocao Lu ◽  
Bu Htan ◽  
...  

2010 ◽  
Vol 16 (35) ◽  
pp. 10818-10831 ◽  
Author(s):  
M. Laura Soriano ◽  
Joseph T. Lenthall ◽  
Kirsty M. Anderson ◽  
Stephen J. Smith ◽  
Jonathan W. Steed

2004 ◽  
Vol 08 (01) ◽  
pp. 67-75 ◽  
Author(s):  
Hiromitsu Maeda ◽  
Hiroyuki Furuta

The peripheral nitrogen of N -confused porphyrins ( NCP ) can serve as a hydrogen bonding donor and acceptor, and a metal coordination site as well. NCP forms versatile dimers with the assistance of metal ions such as Pd II, Pt II, Zn II, Cd II, Hg II, Mn II and Fe II. The square-planar divalent metal complexes of C 6 F 5-substituted NCP with Cu II, Ni II and Pd II act as efficient anion binding receptors. The doubly N -confused porphyrins ( N 2 CP ), possessing both N and NH at the periphery, form self-assembled 1-D hydrogen bonding networks, whose orientations differ in cis (zigzag) and trans (straight) isomers.


2017 ◽  
Vol 73 (6) ◽  
pp. 492-497 ◽  
Author(s):  
S. S. Anjana ◽  
Babu Varghese ◽  
Edamana Prasad

Phosphate esters provide a rigid and stable polymeric backbone in nucleic acids. Metal complexes with phosphate ester groups have been synthesized as structural and spectroscopic models of phosphate-containing enzymes. Dinucleating ligands are used extensively to synthesize model complexes since they provide the support required to stabilize such complexes. The crystal structures of two dinuclear CoII complexes, namely bis(μ-diphenyl phosphato-κ2 O:O′)bis({2-methoxy-N,N-bis[(pyridin-2-yl)methyl]aniline-κ4 N,N′,N′′,O}cobalt(II)) bis(perchlorate), [Co(C12H10O4P)2(C19H19N3O)2](ClO4)2, and bis(μ-diphenyl phosphato-κ2 O:O′)bis({N,N-bis[(pyridin-2-yl)methyl]quinolin-8-amine-κ4 N,N′,N′′,O}cobalt(II)) bis(perchlorate), [Co(C12H10O4P)2(C21H18N4)2](ClO4)2, with tetradentate 2-methoxy-N,N-bis[(pyridin-2-yl)methyl]aniline (L 1) and N,N-bis[(pyridin-2-yl)methyl]quinolin-8-amine (L 2) ligands are reported. The complexes have similar structures, with distorted octahedral geometries around the metal centres. Both are centrosymmetric (Z′ = 0.5), with the CoII centres doubly bridged by diphenyl phosphate ester groups. A number of aromatic–aromatic interactions are present and differ between the two complexes as the anisole group in L 1 is replaced by a quinoline group in L 2. A detailed study of these interactions is presented.


2014 ◽  
Vol 110 ◽  
pp. 169-192 ◽  
Author(s):  
Andrea Bencini ◽  
Francesco Bartoli ◽  
Claudia Caltagirone ◽  
Vito Lippolis

2007 ◽  
Vol 403 (1) ◽  
pp. 43-48 ◽  
Author(s):  
Ali G. Khan ◽  
Stephen R. Shouldice ◽  
Leslie W. Tari ◽  
Anthony B. Schryvers

The acquisition of iron from transferrin by Gram-negative bacterial pathogens is dependent on a periplasmic ferric-ion-binding protein, FbpA. FbpA shuttles iron from the outer membrane to an inner membrane transport complex. A bound phosphate anion completes the iron co-ordination shell of FbpA and kinetic studies demonstrate that the anion plays a critical role in iron binding and release in vitro. The present study was initiated to directly address the hypothesis that the synergistic anion is required for transport of iron in intact cells. A series of site-directed mutants in the anion-binding amino acids of the Haemophilus influenzae FbpA (Gln-58, Asn-175 and Asn-193) were prepared to provide proteins defective in binding of the phosphate anion. Crystal structures of various mutants have revealed that alteration of the C-terminal domain ligands (Asn-175 or Asn-193) but not the N-terminal domain ligand (Gln-58) abrogated binding of the phosphate anion. The mutant proteins were introduced into H. influenzae to evaluate their ability to mediate iron transport. All of the single site-directed mutants (Q58L, N175L and N193L) were capable of mediating iron acquisition from transferrin and from limiting concentrations of ferric citrate. The results suggest that the transport of iron by FbpA is not dependent on binding of phosphate in the synergistic anion-binding site.


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