80528-41-2

Usage

Uses

Used in Analytical Chemistry:
2,6-Bis[bis(2-pyridylMethyl)aMino]Methyl-4-Methylphenol is used as a bidentate ligand for forming stable complexes with metal ions, particularly copper(I), in analytical chemistry. This property allows it to be employed in spectrophotometry, electrochemistry, and fluorescence sensing, enhancing the detection and analysis of metal ions in various samples.
Used in Synthesis of Metal-Based Organic Materials:
In the field of materials science, 2,6-Bis[bis(2-pyridylMethyl)aMino]Methyl-4-Methylphenol is used as a component in the synthesis of metal-based organic materials. Its ability to form stable complexes with metal ions contributes to the development of new materials with unique properties and potential applications.
Used as a Stabilizer in Copper Nanoparticle Production:
2,6-Bis[bis(2-pyridylMethyl)aMino]Methyl-4-Methylphenol is used as a stabilizer in the production of copper nanoparticles. Its complexation with copper ions helps in controlling the size and shape of the nanoparticles, which is crucial for their performance in various applications.
Used in Pharmaceutical Industry:
Although still under investigation, 2,6-Bis[bis(2-pyridylMethyl)aMino]Methyl-4-Methylphenol has been studied for its potential antioxidant and anti-inflammatory properties. If proven effective, it may find future applications in the pharmaceutical industry for the development of drugs targeting oxidative stress and inflammation-related conditions.

Upstream product

• 106-44-5 p-cresol 
• 1539-42-0 bis[(2-pyridyl)methyl]amine 
• 5862-32-8 2,6-bis(chloromethyl)-4-methylphenol 
• 1282615-83-1 2-((pyridin-2-ylmethylamino)methyl)-5-(4-vinylbenzyloxy)phenol 
• 91-04-3 2,6-bis(hydroxymethyl)-4-methylphenol 
• 50-00-0 formaldehyd 

Downstream Products

• 862686-83-7 [Ni₂(2,6-bis(N,N-di(2-pyridylmethyl)aminomethyl)-4-methylphenolate)(bis(p-nitrophenyl) phosphate)2]ClO₄ 
• 862686-85-9 [Zn₂(2,6-bis(N,N-di(2-pyridylmethyl)aminomethyl)-4-methylphenolate)(bis(p-nitrophenyl) phosphate)2]ClO₄ 
• 862686-81-5 [Mn₂(2,6-bis(N,N-di(2-pyridylmethyl)aminomethyl)-4-methylphenolate)(bis(p-nitrophenyl) phosphate)2]ClO₄ 

Relevant academic research and scientific papers

SYNTHESIS AND PROPERTIES OF BINUCLEAR COBALT(II) OXYGEN ADDUCT WITH 2,6-BIS-4-METHYLPHENOL

Binuclear cobalt(II) complexes, ClO4 and (ClO4)2 with 2,6-bis-4-methylphenol (Hbpmp), were prepared.The complexes showed the reversible oxygenation in various solvents.Two to one (Co/

Synthesis and properties of a heterobimetallic iron-manganese complex and its comparison with homobimetallic analogues

Heterobimetallic cofactors containing one manganese and one iron ion have recently been found within the di-metal carboxylate protein family. Herein we report the synthesis and characterization of three binuclear metal complexes with Fe-Fe, Mn-Mn, and Fe-Mn metal composition. All three complexes use the same ligand framework, the BPMP ligand (HBPMP = 2,6-bis[(bis (-2-pyridylmethyl)amine) methyl]-4-methylphenol)) with two additional acetate ligands bridging the two metals. In terms of stability towards metal exchange, the Fe-Mn is more stable than the Mn-Mn complex but less stable than the Fe-Fe complex. Cyclic voltammetry shows that the Fe-Mn complex behaves markedly different than the homobimetallic complexes. The Fe-Mn complex also shows higher reactivity with O2 than both the Fe-Fe and the Mn-Mn counterparts.

The Semireduced Mechanism for Nitric Oxide Reduction by Non-Heme Diiron Complexes: Modeling Flavodiiron Nitric Oxide Reductases

Flavodiiron nitric oxide reductases (FNORs) are a subclass of flavodiiron proteins (FDPs) capable of preferential binding and subsequent reduction of NO to N2O. FNORs are found in certain pathogenic bacteria, equipping them with resistance to nitrosative stress, generated as a part of the immune defense in humans, and allowing them to proliferate. Here, we report the spectroscopic characterization and detailed reactivity studies of the diiron dinitrosyl model complex [Fe2(BPMP)(OPr)(NO)2](OTf)2 for the FNOR active site that is capable of reducing NO to N2O [Zheng et al., J. Am. Chem. Soc. 2013, 135, 4902-4905]. Using UV-vis spectroscopy, cyclic voltammetry, and spectro-electrochemistry, we show that one reductive equivalent is in fact sufficient for the quantitative generation of N2O, following a semireduced reaction mechanism. This reaction is very efficient and produces N2O with a first-order rate constant k > 102 s-1. Further isotope labeling studies confirm an intramolecular N-N coupling mechanism, consistent with the rapid time scale of the reduction and a very low barrier for N-N bond formation. Accordingly, the reaction proceeds at -80 °C, allowing for the direct observation of the mixed-valent product of the reaction. At higher temperatures, the initial reaction product is unstable and decays, ultimately generating the diferrous complex [Fe2(BPMP)(OPr)2](OTf) and an unidentified ferric product. These results combined offer deep insight into the mechanism of NO reduction by the relevant model complex [Fe2(BPMP)(OPr)(NO)2]2+ and provide direct evidence that the semireduced mechanism would constitute a highly efficient pathway to accomplish NO reduction to N2O in FNORs and in synthetic catalysts.

Influence of the metals and ligands in dinuclear complexes on phosphopeptide sequencing by electron-transfer dissociation tandem mass spectrometry

Phosphorylation is one of the most important protein modifications, and electron-transfer dissociation tandem mass spectrometry (ETD-MS/MS) is a potentially useful method for the sequencing of phosphopeptides, including determination of the phosphorylatio

Design of coordination interaction of Zn(II) complex with oligo-aspartate peptide to afford a high-affinity tag-probe pair

A complementary recognition pair consisting of a genetically encodable peptide tag and a small molecular probe isa powerful tool to specifically label and manipulate a protein ofinterest under biological conditions. In this study, we report the redesign of a tag-probe pair comprising an oligo-aspartate peptide tag (such as DDDD) and a binuclear zinc complex. Isothermal-titration calorimetry screening of binding between the series of peptides and zinc complexes revealed that the binding affinity was largely influenced by subtle changes of the ligand structure of the probe. However, the binding was tolerant to differences of the tag peptide sequence. Of those tested, a pair containing a peptide tag (DDAADD) and a binuclear zinc complex possessing 4-chloropyridines (3-2Zn(II)) showed the strongest binding affinity (Ka = 3.88 × 105 M-1), which was about 10-fold larger than the conventional pair of D4-peptide tag (DDDD) and 1-2Zn(II) containing nonsubstituted pyridines (Ka = 3.73 × 104 M-1). The strong binding of this new complementary recognition pair enabled the rapid covalent labeling of a tag-fused maltose binding protein with a fluorescent zinc complex, demonstrating its potential utility in protein analysis.

Molecular recognition and scavenging of arsenate from aqueous solution using dimetallic receptors

A series of copper(II), nickel(II) and zinc(II) dimetallic complexes were prepared and their affinities towards arsenate investigated. Indicator displacement assays (IDAs) were carried out to establish the complexes with best affinities towards arsenate.

A potentially polymerizable heterodinuclear FeIIIZnII purple acid phosphatase mimic. Synthesis, characterization, and phosphate ester hydrolysis studies

An analogue of the purple acid phosphatase biomimetic 2-((bis(pyridin-2- ylmethyl)amino)methyl)-6-(((2-hydroxybenzyl)(pyridin-2-ylmethyl)amino)methyl) -4-methylphenol has been synthesized. The analogue, 2-((bis(pyridin-2-ylmethyl) amino)methyl)-6-(((2-hydroxy-4-(4-vinylbenzyloxy)benzyl)(pyridin-2-ylmethyl) amino)methyl)-4-methylphenol (H2BPBPMPV) possesses a pendant olefin suitable for copolymerization. Complexation with FeIII/Zn II resulted in the complex [FeIIIZnII(BPBPMPV) (CH3COO)2](ClO4), characterized with mass spectrometry, microanalysis, UV/vis, and IR spectrometry. The catalytic activity of the complex toward bis-(2,4-dinitrophenyl) phosphate was determined, resulting in Km of 4.10.6mM, with kcat 3.80.210 -3s-1 and a bell-shaped pHrate profile with pKa values of 4.31, 5.66, 8.96, the profile exhibiting residual activity above pH 9.5. CSIRO 2011.

Hydrogen-bond promoted intramolecular electron transfer to photogenerated Ru(III): A functional mimic of tyrosine(z) and histidine 190 in photosystem II

As a model for redox components on the donor side of photosystem II (PS II) in green plants, a supramolecular complex 4 has been prepared. In this, a ruthenium(II) tris-bipyridyl complex which mimics the function of P680 in PS II, has been covalently linked to a tyrosine unit which bears two hydrogen-bonding substituents, dipicolylamine (dpa) ligands. Our aim is to mimic the interaction between tyrosine(z) and a basic histidine residue, namely His190 in PSII, and also to use the dpa ligands for coordination of manganese. Two different routes for the synthesis of the compound 4 are presented. Its structure was fully characterized by 1H NMR, COSY, NOESY, 13C NMR, IR, and mass spectrometry. 1H NMR and NOESY gave evidence for the existence of intramolecular hydrogen bonding in 4. The interaction between the ruthenium and the substituted tyrosine unit was probed by steady-state and time-resolved emission measurements as well as by chemical oxidation. Flash photolysis and EPR measurements on 4 in the presence of an electron acceptor (methylviologen, MV2+, or cobalt pentaminechloride, Co3+) showed that an intermolecular electron transfer from the excited state of Ru(II) in 4 to the electron acceptor took place, forming Ru(III) and the methylviologen radical MV+· or Co2+. This was followed by intramolecular electron transfer from the substituted tyrosine moiety to the photogenerated Ru(m), regenerating Ru(II) and forming a tyrosyl radical. In water, the radical has a g value of 2.0044, indicative of a deprotonated tyrosyl radical. In acetonitrile, a radical with a g value of 2.0029 was formed, which can be assigned to the tyrosine radical cation. In both solvents the electron transfer is intramolecular with a rate constant κ(ET) > 1 x 107 s-1. This is 2 orders of magnitude greater than the one for a similar compound 3, in which no dpa arm is attached to the tyrosine unit. Therefore the hydrogen bonding between the substituted tyrosine and the dpa arms in 4 is proposed to be responsible for the fast electron transfer. This interaction mimics the proposed His190 and tyrosine(z) interaction in the donor side of PS II.

A New Method for the Synthesis of Nonsymmetric Dinucleating Ligands by Aminomethylation of Phenols and Salicylaldehydes

Monoaminomethylated phenols 5-7 and symmetrically diaminomethylated phenols 8 and 9 were prepared in a one-step procedure from p-cresol, formaldehyde, and a variety of secondary amines by making use of the aromatic Mannich reaction.Nonsymmetric diaminomet

Models for Iron-Oxo Proteins. Structures and Properties of Fe(II)Fe(III), Zn(II)Fe(III), and Fe(II)Ga(III) Complexes with (μ-Phenoxo)bis(μ-carboxylato)dimetal Cores

A series of bimetallic complexes, X2 where BPMP is the anion of 2,6-bis-4-methylphenol, has been synthesized to provide models for binuclear metal-oxo centers in proteins (1, M = M' = Fe, R = C2H