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Mn(III)TMPyP

目录号 : GC44239

A SOD mimetic and peroxynitrite decomposition catalyst

Mn(III)TMPyP Chemical Structure

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产品描述

Mn(III)TMPyP is a manganese-porphyrin which acts as a superoxide dismutase (SOD) mimetic and peroxynitrite decomposition catalyst. SOD mimetics described to date are unstable and are capable of catalyzing undesired side-reactions in addition to the dismutation of the superoxide radical (O2-). Mn(III)TMPyP is an SOD mimetic with increased stability to pH and hydrogen peroxide. The rate constant for superoxide dismutation and peroxynitrite decomposition are 3.9 x 107 M-1s-1 and ~2 x 106 M-1s-1, respectively. Mn(III)TMPyP protected and enhanced the growth of SOD null E. coli with a doubling time of 60 minutes (as compared to 240 minutes of the control) at 25 µM.

Chemical Properties

Cas No. SDF
化学名 Mn(III)tetrakis(1-methyl-4-pyridyl)porphyrin pentachloride
Canonical SMILES C[n]1ccc(cc1)C1=c2ccc3C(=c4ccc5=C(c6cc[n](C)cc6)c6ccc7=C(c8cc[n](C)cc8)c8ccc1n8[Mn]([n]23)([n]67)n45)c1cc[n](C)cc1
分子式 C44H36MnN8 • 5Cl 分子量 909
溶解度 Soluble at concentration of at least 50mg/mL in 0.1 M Tris-HCI buffer (1 mM EDTA, pH 9.0), and 4mg/mL in PBS (pH 7.2) 储存条件 Store at -20°C
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1 mM 1.1001 mL 5.5006 mL 11.0011 mL
5 mM 0.22 mL 1.1001 mL 2.2002 mL
10 mM 0.11 mL 0.5501 mL 1.1001 mL
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Research Update

Antioxidant cytochrome c-like activity of para-Mn(III)TMPyP

Biochimie 2021 May;184:116-124.PMID:33662439DOI:10.1016/j.biochi.2021.02.015.

Manganese porphyrins are well-known protectors against the deleterious effects of pro-oxidant species such as superoxide ions and hydrogen peroxide. The present study investigated the antioxidant cytochrome c-like activities of Mn(III)TMPyP [meso-tetrakis (4-N-methyl pyridinium) porphyrin] against superoxide ion and hydrogen peroxide that remained unexplored for this porphyrin. The association of TMPyP with a model of the inner mitochondrial membrane, cardiolipin (CL)-containing liposomes, shifted +30 mV vs. NHE (normal hydrogen electrode) redox potential of the Mn(II)/Mn(III) redox couple. In CL-containing liposomes, Mn(III)TMPyP was reduced by superoxide ions and recycled by Fe(III)cytochrome c to the oxidized form. Similarly, isolated rat liver mitoplasts added to a sample of Mn(II)TMPyP promoted immediate porphyrin reoxidation by electron transfer to the respiratory chain. These results show that Mn(III)TMPyP can act as an additional pool of Fe(III)cytochrome c capable of transferring electrons that escape from the IV complex back into the respiratory chain. Unlike Fe(II)cytochrome c, Mn(II)TMPyP was not efficient for hydrogen peroxide clearance. Therefore, by reducing cytochrome c, Mn(II)TMPyP can indirectly contribute to hydrogen peroxide elimination.

Superoxide scavenging by Mn(II/III) tetrakis (1-methyl-4-pyridyl) porphyrin in mammalian cells

Arch Biochem Biophys 1996 Jan 1;325(1):20-8.PMID:8554339DOI:10.1006/abbi.1996.0003.

The superoxide dismutase mimic Mn(II/III) tetrakis (1-methyl-4-pyridyl) porphyrin (Mn(II/III)TMPyP) was examined for its superoxide radical (O2.-)-scavenging ability in cultured mammalian cells. Mn(III)TMPyP (< 5 microM) added to culture media relieved growth inhibition and decreased the inactivation of the O2(.-)-sensitive enzyme aconitase in cells exposed to the O2(.-)-generating phenazine pyocyanine. Treatment of cells with Mn(III)TMPyP did not measurably affect cellular O2.- production as revealed by rates of cyanide-resistant respiration with or without added pyocyanine. In contrast, Mn(II/III)TMPyP enhanced O2.- production in cells when the redox-active naphthoquinone menadione was present as measured by both increased cyanide-resistant respiration rates and aconitase inactivation. In vitro, Mn(II/III)TMPyP catalyzed the oxidation of ascorbate, and menadione enhanced this effect. Mn(III)TMPyP did not protect aconitase when O2.- production was elicited in mitochondria by antimycin A and the uncoupler carbonyl cyanide p-trifluoromethoxyphenylhydrazone. The results support a reductant-O2.-:oxidoreductase mechanism for O2.- scavenging by Mn(II/III)TMPyP in the mammalian cytosol as proposed for its action in Escherichia coli, but also indicate that Mn(II/III)TMPyP can either scavenge or produce O2.- in cells depending upon the prevailing pathways of Mn(II/III)TMPyP oxidation-reduction.

Binding of the Mn(III) complex of meso-tetrakis (4-N-methyl-pyridiniumyl) porphyrin to DNA. Effect of ionic strength

J Inorg Biochem 1999 Jan-Feb;73(1-2):35-40.PMID:10212993DOI:10.1016/s0162-0134(98)10088-0.

Interactions of the water-soluble Mn(III) complex of meso-tetrakis (4-N-methyl-pyridiniumyl) porphyrin (Mn(III)TMPyP) with DNA in aqueous solutions at low (0.01 M) and high (0.2 M) ionic strengths have been studied by optical absorption, resonance light scattering (RLS) and 1H NMR spectroscopies. Optical absorption and RLS measurements have demonstrated that in DNA solutions at low ionic strength the Mn(III)TMPyP form aggregates, which are decomposed at DNA excess. At high ionic strength the aggregation was not observed. We explain this effect by assuming that upon increase in ionic strength, Mn(III) TMPyP dislocates from the DNA sites, which produces better conditions for the porphyrin aggregation, to sites where the aggregation is hindered. The 1H NMR data demonstrated that the aggregation observed at low ionic strength reduces the paramagnetism of Mn(III)TMPyP. This phenomenon was not observed at the high ionic strength in the absence of aggregation.

Opposite effects of Mn(III) and Fe(III) forms of meso-tetrakis(4-N-methyl pyridiniumyl) porphyrins on isolated rat liver mitochondria

J Bioenerg Biomembr 2002 Feb;34(1):41-7.PMID:11860179DOI:10.1023/a:1013818719932.

The relevance of porphyrins as therapeutic drugs targeted to mitochondria has been widely recognized. In this work, we studied the action of meso-tetrakis porphyrins (TMPyP) on respiring rat liver mitochondria. Mn(III)TMPyP exerted a protective effect against lipid peroxidation induced by Fe(II) or the azo initiator 4,4'-azobis(4-cyanopentanoic acid) (ABCPA), which partition in the hydrophobic phospholipid moiety, and 2,2'-azobis(2-amidinepropane)dihydrochloride (ABAP), which partitions in the aqueous phase. In contrast, Fe(III)TMPyP itself induced an intense lipid peroxidation, accompanied by mitochondrial permeability transition. Both mesoporphyrins studied promoted a release of mitochondrial state-4 respiration, in the concentration range of 1.0-20 microM. Based on the relative effects of Mn(III)TMPyP against ABAP and ABCPA-induced lipid peroxidation, we believe that meso-tetrakis porphyrins must concentrate preferably at membrane-water interfaces.

Towards the mechanisms involved in the antioxidant action of MnIII [meso-tetrakis(4-N-methyl pyridinium) porphyrin] in mitochondria

J Bioenerg Biomembr 2011 Dec;43(6):663-71.PMID:21986957DOI:10.1007/s10863-011-9382-3.

Aerobic organisms are afforded with an antioxidant enzymatic apparatus that more recently has been recognized to include cytochrome c, as it is able to prevent hydrogen peroxide generation by returning electrons from the superoxide ion back to the respiratory chain. The present study investigated the glutathione peroxidase (GPx), superoxide dismutase (SOD) and cytochrome c-like antioxidant activities of para Mn(III)TMPyP in isolated rat liver mitochondria (RLM) and mitoplasts. In RLM, Mn(III)TMPyP decreased the lipid-peroxide content associated with glutathione (GSH) depletion consistent with the use of GSH as a reducing agent for high valence states of Mn(III)TMPyP. SOD and cytochrome c antioxidant activities were also investigated. Mn(II)TMPyP was able to reduce ferric cytochrome c, indicating the potential to remove a superoxide ion by returning electrons back to the respiratory chain. In antimicyn A-poisoned mitoplasts, Mn(III)TMPyP efficiently decreased the EPR signal of DMPO-OH adduct concomitant with GSH depletion. The present results are consistent with SOD and GPx activities for Mn(III)TMPyP and do not exclude cytochrome c-like activity. However, considering that para Mn(III)TMPyP more efficiently reduces, rather than oxidizes, superoxide ion; electron transfer from the Mn(II)TMPyP to the respiratory chain might not significantly contribute to the superoxide ion removal, since most of Mn(II)TMPyP is expected to be produced at the expense of NADPH/GSH oxidation. The present results suggest GPx-like activity to be the principal antioxidant mechanism of Mn(III)TMPyP, whose efficiency is dependent on the NADPH/GSH content in cells.