87261-81-2

Upstream product

• 1600-27-7 mercury(II) diacetate 
• 142-71-2 copper diacetate 
• 84752-34-1 (N-methyltetrakis(p-sulfophenyl)porphinato)copper(II)^(3-) 
• 109-89-7 diethylamine 
• 35218-75-8 5,10,15,20-tetrakis(4-sulfonatophenyl)porphyrin 

Relevant academic research and scientific papers

Direct Structural Determination of the Short-lived Intermediate Formed in the Dynamic Incorporation of a Copper(II) Ion into a Mercury(II) Porphyrin by the Stopped-flow EXAFS Method

Structure parameters around the CuII ion in a reaction intermediate formed in the course of CuII ion incorporation into an HgII porphyrin were directly determined using a new stopped-flow EXAFS apparatus, and elongation of the Cu-N bond in the unstable heterodinuclear porphyrin intermediate was observed.

Single-molecule porphyrin-metal ion interaction and sensing application

It remains a significant challenge to study the interactions between metal ions and porphyrin molecules at single ion level. Here, we constructed a nanopore-based sensing for label-free and real-time analysis of the interaction between Cu2+ and

Reactions of Water-Soluble Metalloporphyrins with the Serum Protein, Hemopexin

Rabbit hemopexin is capable of binding a wide variety of synthetic porphyrins and metalloporphyrins including those of the meso-substituted variety.The protein has a requirement for negatively charged peripheral substituents on the porphyrin suggesting that the binding site(s) have a residual positive charge.The stable porphyrin-protein complexes are 1:1 and involve monomeric porphyrin units regardless of the state of aggregation of the porphyrin in solution.The kinetics of the reactions of tetra(4-sulfonatophenyl)porphinatoferrate(III) (FeIIITPPS) with rabbit hemopexin has been studied as a function of pH.The protein is capable of interacting with either monomers or dimers leading to substantial changes in metalloporphyrin absorbance and protein fluorescence.When the bound FeIIITPPS is dimeric, a much slower process ensues in which the intermediate complex loses a monomer unit to form the stable product.

Association of Small Molecule Cosolutes with Water-Soluble Polymers. Effects of Polymer Binding on the Reactivity of Water-Soluble Porphyrins

The tetraanionic porphyrin, 1, associates strongly with poly(vinylpyrrolidone) (PVP) in dilute buffered aqueous solutions.The equilibrium constant for association of 1 with PVP in pH 3 acetate at 298 K is 1.4 x 1E7 M-1 for M = 48000 PVP.Chelation of Cu2+ by the porphyrin is slowed dramatically in the presence of PVP.The rate expression is Kb2+>/(k' + k 2+>), which fits a mechanism in which only free porphyrin, f, coordinates to Cu2+ (b is the concentration of polymer-bound porphyrin).The palladium(II) porphyrin, 2, also associates with PVP.The palladium(II) porphyrin, 2, also associates with PVP.The efficient quenching of the phosphorescence of 2 by methylviologen, MV2+, in aqueous solution is completely inhibited upon association of 2 with PVP.The lack of reactivity of 1 and 2 bound to PVP indicates that the porphyrin microenvironment involves little contact with the bulk aqueous solution.

Catalytic unfolding and proteolysis of cytochrome c induced by synthetic binding agents

A class of polyanionic copper porphyrin dimers is shown to selectively increase the susceptibility of cytochrome c to proteolysis through binding-induced disruption of tertiary and secondary structure. The free energy of the protein conformation leading to proteolytic attack is stabilized by about 2.4 kcal/mol in the bound state. The proteolytic acceleration is catalytic in nature, requiring only a fraction of an equivalent of metalloporphyrin to effect complete, rapid digestion in the presence of a protease.

Kinetic Studies on Metalloporphyrin Formation in Aqueous Solutions of meso-Tetra(p-sulphonatophenyl)-porphyrin and some Metal(II) Ions

Studies on kinetics of metalloporphyrin formation in weakly acidic aqueous solution (pH 3.8-4.7) in perchlorate medium have been carried out spectrophotometrically at 435 nm for the reactions of M(H2O)62+ (M = Mn, Fe, Co, Ni, Cu) with meso-tetra(p-sulphonatophenyl)prophyrin, TPPS4-. The results have been compared with the corresponding reactions of meso-tetra(4-N-methylpyridyl)porphyrin and the water exchange rates of the aqua-metal(II) ions. Compared to water exchange rates, reduction in the rate of formation of metalloporphyrin with TPPS4- is by a factor of 107 to 1010, the minimum and maximum values being observed with NiII and MnII respectively. The results have been interpreted on the basis of the general mechanism for metalloporphyrin formation.