Structure of monomeric hydrated manganese(III) tetra(4-N-methylpyridyl)porphyrin pentachloride

Prince, Stephen M.; Körber, F.; Cooke, Paul R.; Smith, John R. Lindsay; Mazid, Muhammed A.

doi:10.1107/s0108270193000447

Cited by 26 publications

(20 citation statements)

References 3 publications

(3 reference statements)

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“…Furthermore, the nickel porphyrins are expected to interact by stacking, whereas stacking interactions are impossible for manganese porphyrins due to the presence of water as axial ligands on the manganese. [31] The binding of these porphyrin derivatives to duplex and intramolecular quadruplex DNA was studied by surface plasmon resonance, and their capacity to inhibit telomerase was measured by TRAP assays. The data show that, within this series of metalloporphyrin derivatives, the kinetics of binding to DNA (k on , k off ) were highly dependent on the nature of the central metal.…”

Section: Introductionmentioning

confidence: 99%

Porphyrin Derivatives for Telomere Binding and Telomerase Inhibition

et al. 2005

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The capacity of G-quadruplex ligands to stabilize four-stranded DNA makes them able to inhibit telomerase, which is involved in tumour cell proliferation. A series of cationic metalloporphyrin derivatives was prepared by making variations on a meso-tetrakis(4-N-methyl-pyridiniumyl)porphyrin skeleton (TMPyP). The DNA binding properties of nickel(II) and manganese(III) porphyrins were studied by surface plasmon resonance, and the capacity of the nickel porphyrins to inhibit telomerase was tested in a TRAP assay. The nature of the metal influences the kinetics (the process is faster for Ni than for Mn) and the mode of interaction (stacking or external binding). The chemical alterations did not lead to increased telomerase inhibition. The best selectivity for G-quadruplex DNA was observed for Mn-TMPyP, which has a tenfold preference for quadruplex over duplex.

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Section: Introductionmentioning

confidence: 99%

Porphyrin Derivatives for Telomere Binding and Telomerase Inhibition

et al. 2005

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“…[18,19] The molecular structure of [(4') Mn] 2+ in the respective crystal ( Figure 1) Mn] 2+ moieties form dimers in the crystal with relatively close contacts between the concave sides of the two species, which face one another (an entire dimer also comprises the asymmetric unit of the structure). Thus, the nonbonding distances between the nearly overlapping C atoms of the macrocyclic core in the two units are within 3.4-3.6 , and the distance between the corresponding Mn ion centers is 4.17 .…”

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confidence: 99%

“…Four nitrogen atoms define the equatorial plane in both complexes, but a full charge balance exists in the latter case only. Manganese porphyrin complexese require at least one strongly bound axial ligand, [18,19] which is considered the main obstacle for intercalation. [21] On the other hand, the molecular structure of [(4')Mn] 2+ reveals only one axially coordinated solvent molecule; four-coordinated manganese-(III) corroles have been reported as well.…”

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confidence: 99%

DNA Binding and Catalytic Properties of Positively Charged Corroles

2007

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“…In the second step, one of the N-methylpyridinium-4-yl pendant groups was attached in the meso position of the porphyrin, in agreement with the crystallographic structure of Mn(III)-TMPyP. 29 In the first step the 6-31G* basis set was used for H, C, N, and O atoms and the full geometry optimization and frequency calculations were carried out. For the second step, the porphyrin with the N-methylpyridinium-4-yl substituents, due to the size of the system, the basis set for H, C, N, and O atoms was reduced to 3-21G*.…”

Section: Structure Charge and Amber Force Field Parametersmentioning

confidence: 99%

Theoretical study of the interaction between a high‐valent manganese porphyrin oxyl‐(hydroxo)‐Mn(IV)‐TMPyP and double‐stranded DNA

2003

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Cationic porphyrin derivatives such as meso-tetrakis(4-N-methylpyridinium)porphyrin, TMPyP, have been shown to interact with double-stranded DNA. The manganese derivative, Mn(III)-TMPyP, activated by an oxygen donor like potassium monopersulfate, provides an efficient DNA-cleaving system. Previous experimental work1 has shown that DNA cleavage by the Mn(III)-TMPyP/KHSO(5) system was due to an oxidative attack, within the minor groove of B-DNA, at the C5' or C1' carbons of deoxyribose units. The aim of this study was to use molecular modeling to elucidate the specificity of the interactions between the transient active species oxyl-Mn(IV)-TMPyP and the DNA target. Geometric parameters, charges, and force field constants consistent with the AMBER 98 force field were calculated by DFT methods. Molecular modeling (mechanics and dynamic simulations) were performed for oxyl-(hydroxo)-Mn(IV)-TMPyP bound in the minor groove of the dodecamer d(5'-TCGTCAAACCGC)-d(5'-GCGGTTTGACGA). Geometry, interactions, and binding energy of the metalloporphyrin located at the A.T triplet region of the dodecamer were analyzed. These studies show no significant structural change of the DNA structure upon ligand binding. Mobility of the metalloporphyrin in the minor groove was restrained by the formation of a hydrogen bond between the hydroxo ligand trans to the metal-oxyl and a DNA phosphate, restricting the access of the oxyl group to the (pro-S) H atom at C5'.

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Structure of monomeric hydrated manganese(III) tetra(4-N-methylpyridyl)porphyrin pentachloride

Cited by 26 publications

References 3 publications

Porphyrin Derivatives for Telomere Binding and Telomerase Inhibition

Porphyrin Derivatives for Telomere Binding and Telomerase Inhibition

DNA Binding and Catalytic Properties of Positively Charged Corroles

Theoretical study of the interaction between a high‐valent manganese porphyrin oxyl‐(hydroxo)‐Mn(IV)‐TMPyP and double‐stranded DNA

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