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¹¹³Cd as a Probe in NMR Studies of Allosteric Host-Guest-Ligand Complexes of Porphyrin Cage Compounds.

ABSTRACT: Cadmium porphyrin cage compounds Cd1 and ¹¹³ Cd1 have been synthesized from the free base porphyrin cage derivative H₂1 and Cd(OAc)₂ ⋅ 2 H₂O or ¹¹³Cd(OAc)₂ ⋅ 2 H₂O, respectively. The compounds form allosteric complexes with the positively charged guests N,N'-dimethylimidazolium hexafluorophosphate (DMI) and N,N'-dimethylviologen dihexafluorophosphate (Me₂V), which bind in the cavity of the cage, and tbupy, which coordinates as an axial ligand to the outside of the cage. In the presence of tbupy, the binding of DMI in Cd1 is enhanced by a factor of ∼31, while the presence of DMI or Me₂V in the cavity of Cd1 enhances the binding of tbupy by factors of 55 and 85, respectively. The X-ray structures of the coordination complexes of Cd1 with acetone, acetonitrile, and pyridine, the host-guest complex of Cd1 with a bound viologen guest, and the ternary allosteric complex of Cd1 with a bound DMI guest and a coordinated tbupy ligand, were solved. These structures revealed relocations of the cadmium center in and out of the porphyrin plane, depending on whether a guest or a ligand is present. ¹¹³Cd NMR could be employed as a tool to quantify the binding of guests and ligands to ¹¹³ Cd1. 1D EXSY experiments on the ternary allosteric system Cd1-tbupy-Me₂V revealed that the coordination of tbupy significantly slowed down the dissociation of the Me₂V guest. Eyring plots of the dissociation process revealed that this kinetic allosteric effect is entropic in nature.

SUBMITTER: Bruekers JPJ

PROVIDER: S-EPMC9324901 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature

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113Cd as a Probe in NMR Studies of Allosteric Host-Guest-Ligand Complexes of Porphyrin Cage Compounds.

Bruekers Jeroen P J JPJ Hellinghuizen Matthijs A MA Swartjes Anne A Tinnemans Paul P White Paul B PB Elemans Johannes A A W JAAW Nolte Roeland J M RJM

European journal of organic chemistry 20220413 15

Cadmium porphyrin cage compounds Cd1 and 113 Cd1 have been synthesized from the free base porphyrin cage derivative H21 and Cd(OAc)2 ⋅ 2 H2O or 113Cd(OAc)2 ⋅ 2 H2O, respectively. The compounds form allosteric complexes with the positively charged guests N,N'-dimethylimidazolium hexafluorophosphate (DMI) and N,N'-dimethylviologen dihexafluorophosphate (Me2V</ ...[more]

PMID: 35915641

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Project description:Our laboratories have actively published in this area for several years and the objective of this chapter is to present as comprehensive an overview as possible. Following a brief review of the basic principles associated with (113)Cd NMR methods, we will present the results from a thorough literature search for (113)Cd chemical shifts from metalloproteins. The updated (113)Cd chemical shift figure in this chapter will further illustrate the excellent correlation of the (113)Cd chemical shift with the nature of the coordinating ligands (N, O, S) and coordination number/geometry, reaffirming how this method can be used not only to identify the nature of the protein ligands in uncharacterized cases but also the dynamics at the metal binding site. Specific examples will be drawn from studies on alkaline phosphatase, Ca(2+) binding proteins, and metallothioneins.In the case of Escherichia coli alkaline phosphatase, a dimeric zinc metalloenzyme where a total of six metal ions (three per monomer) are involved directly or indirectly in providing the enzyme with maximal catalytic activity and structural stability, (113)Cd NMR, in conjunction with (13)C and (31)P NMR methods, were instrumental in separating out the function of each class of metal binding sites. Perhaps most importantly, these studies revealed the chemical basis for negative cooperativity that had been reported for this enzyme under metal deficient conditions. Also noteworthy was the fact that these NMR studies preceded the availability of the X-ray crystal structure.In the case of the calcium binding proteins, we will focus on two proteins: calbindin D(9k) and calmodulin. For calbindin D(9k) and its mutants, (113)Cd NMR has been useful both to follow actual changes in the metal binding sites and the cooperativity in the metal binding. Ligand binding to calmodulin has been studied extensively with (113)Cd NMR showing that the metal binding sites are not directly involved in the ligand binding. The (113)Cd chemical shifts are, however, exquisitely sensitive to minute changes in the metal ion environment.In the case of metallothionein, we will reflect upon how (113)Cd substitution and the establishment of specific Cd to Cys residue connectivity by proton-detected heteronuclear (1)H-(113)Cd multiple-quantum coherence methods (HMQC) was essential for the initial establishment of the 3D structure of metallothioneins, a protein family deficient in the regular secondary structural elements of α-helix and β-sheet and the first native protein identified with bound Cd. The (113)Cd NMR studies also enabled the characterization of the affinity of the individual sites for (113)Cd and, in competition experiments, for other divalent metal ions: Zn, Cu, and Hg.

Dataset Information

¹¹³Cd as a Probe in NMR Studies of Allosteric Host-Guest-Ligand Complexes of Porphyrin Cage Compounds.

Publications

<sup>113</sup>Cd as a Probe in NMR Studies of Allosteric Host-Guest-Ligand Complexes of Porphyrin Cage Compounds.

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