Hydrogen-bonded supramolecular manganese(II) complexes with network and sheet structures bridged by terephthalate unit

Two 1D complexes [Mn(4- methylpyrazole)₃(H₂O)(tp)]_n (2) and [Mn(4-methylpyrazole)₄(tp)]_n (3) (tp = terephthalate) were synthesized and characterized by means of X-ray analysis and magnetic studies. The molecular structure of 2 reveals that Mn(II) centers with asymmetric coordination surroundings are bridged by crystallographically different tp ligands, forming a 1D chain. The 1D coordination chains are interconnected by hydrogen bonds between free carboxylate oxygen atoms in a chain and hydrogens of pyrazole nitrogen atoms in neighboring chains, leading to a 3D framework. Compound 3 also exhibits a 1D coordination chain which is hydrogen-bonded to adjacent chains, providing a 2D sheet structure. Interestingly, the structures include intra- and interchain hydrogen bonds contributed from N-H groups of the capping 4-methylpyrazole ligands. Magnetic measurements show weak antiferromagnetic interactions with exchange coupling parameters of J = −0.018 cm⁻¹ for 2 and J = −0.062 cm⁻¹ for 3 through the extended tp ligand on the basis of an infinite chain model (H = −J∑S_i · S_i + 1).     

Mechanistic aspects of the Fenton reaction under conditions approximated to the extracellular fluid

The Fenton reaction was investigated, in a medium approximating to that of the extracellular fluid (ECF), by rapid-mixing stopped flow experiments and HPLC analysis using sodium terephthalate (TA²⁻). The reactive intermediate of the Fenton reaction hydroxylates the essentially nonfluorescent, TA²⁻ to the brilliant fluorophor 2-hydroxy-terephthalate (OH-TA), which allows the Fenton reaction to be monitored in stopped-flow experiments. There was no artefactual quenching of the fluorescence by substances present in the Fenton-reaction mixture or in the artificial cerebrospinal fluid (aCSF) that might have influenced OH-TA quantification. A mathematical model based on kinetic considerations was developed. This explains the observed independence of the OH-TA concentration on the amount of TA²⁻ present in aCSF as well as its dependence on TA²⁻ concentration in potassium acetate buffer. A mechanism based on this model, involving complex formation between Fe(II), TA²⁻ and H₂O₂, followed by an intra-molecular hydroxylation accompanied by an intra-molecular electron transfer was developed. The results are consistent with a reactive intermediate, which causes oxidative stress in vivo, not being a free hydroxyl radical, but a ferryl species or a “crypto” radical. The biological implications of these results are discussed.     

Purification and gene cloning of the oxygenase component of the terephthalate 1,2-dioxygenase system from Delftia tsuruhatensis strain T7

The terephthalate 1,2-dioxygenase system (TERDOS) was found in cell extracts of Delftia tsuruhatensis strain T7 (=IFO16741) grown in terephthalate-salt medium. The cell extract was separated by anion exchange chromatography to yield two fractions (R and Z) that were necessary for oxygenation of terephthalate with NADH and Fe(2+). The oxygenase component of TERDOS (TerZ) was purified from fraction Z by gel filtration chromatography to near homogeneity. An alpha(3)beta(3) subunit structure was deduced from the molecular masses of 235, 46 and 17 kDa of the native complex and the alpha- and beta-subunits, respectively. The N-terminal amino acid sequences of the two subunits of TerZ allowed polymerase chain reaction primers to be deduced and the DNA sequence of the alpha-subunit was determined. The amino acid sequence of the alpha-subunit (TerZalpha) showed significant similarities to the large subunits of multicomponent ring-hydroxylating oxygenases. Two motifs in the deduced amino acid sequence, a Rieske [2Fe-2S] center and a mononuclear Fe(II) binding site, were observed. Phylogenetic analyses indicated that TerZalpha and the large oxygenase component subunits ortho-halobenzoate 1,2-dioxygenase and salicylate-5-hydroxylase form a cluster that is distant from the rest of the large oxygenase subunits of multicomponent ring-hydroxylating oxygenases.     

A 3D supramolecular network of cobalt(II)(bis(4-pyridyl)ethylene) with terephthalate dianions

A three dimensional supramolecular network, {[Co(bpee)(H₂O)₄] · (tp) · 2(H₂O)}_n (1) [bpee = trans-1,2 bis(4-pyridyl)ethylene; tp = terephthalate dianion] has been synthesized and characterized by X-ray single crystal structure, magnetic measurement and thermal analysis. The structure determination reveals that the cobalt(II) ions, bridged by bpee and coordinated by four water molecules, give rise to covalently linked 1D polymeric chain. The parallel chains get involved in H-bonding with tp resulting in a 3D architecture. Upon heating 1, which is pink in color, transforms to [Co(bpee)(tp)] (1a, blue). The deaquated species (1a) reverts on keeping in humid atmosphere. Low temperature magnetic data indicate weak antiferromagnetic coupling.     

The detection of hydroxyl radicals in vivo

Several indirect methods have been developed for the detection and quantification of highly reactive oxygen species (hROS), which may exist either as free hydroxyl radicals, bound “crypto” radicals or Fe(IV)-oxo species, in vivo. This review discusses the strengths and weaknesses associated with those most commonly used, which determine the hydroxylation of salicylate or phenylalanine. Chemical as well as biological arguments indicate that neither the hydroxylation of salicylate nor that of phenylalanine can guarantee an accurate hydroxyl radical quantitation in vivo. This is because not all hydroxylated product-species can be used for detection and the ratio of these species strongly depends on the chemical environment and on the reaction time. Furthermore, at least in the case of salicylate, the high concentrations of the chemical trap required (mM) are known to influence biological processes associated with oxidative stress.Two, newer, alternative methods described, the 4-hydroxy benzoic acid (4-HBA) and the terephthalate (TA) assays, do not have these drawbacks. In each case reaction with hROS leads to only one hydroxylated product. Thus, from a chemical viewpoint, they should provide a better hROS quantitation. Further work is needed to assess any possible biological effects of the required millimolar (4-HBA) and micromolar (TA) concentrations of the chemical traps.     

Ferromagnetic interactions in copper(II) and nickel(II) coordination polymers containing nitronyl nitroxide radical and terephthalate

Two new complexes [Cu(NITmPy)₂(tp)] 1 and [Ni(NITmPy)₂(tp)(H₂O)₂] 2 (NITmPy=2-(3^′-pyridyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide and tp=terephthalato dianion) were synthesized and structurally and magnetically characterized. The structure of 1 is a neutral infinite chain where Cu(NITmPy)₂ units are linked by terephthalate ligands. In complex 2, the 1-D chains of Ni(NITmPy)₂ (H₂O)₂ units connected by tp develop into 2-D network via hydrogen bond interactions. The magnetic properties of 1 and 2 have been investigated in the temperature range 2-300 K. Both complexes exhibit ferromagnetic coupling and antiferromagnetic interactions dominate at low temperature. The magnetic behavior is discussed based on their structures.     

Purification and some properties of (1R,2S)-1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase from Comamonas testosteroni T-2

Abstract Inducible (1 R ,2 S )-1,2-dihydroxy-3,5-cyclohexadiene-l,4-dicarboxylate (diene-diol) dehydrogenase was found in extracts of Comamonas testosteroni T-2 grown in p -toluate-or terephthalate-salts medium and it was purified using anion exchange, hydrophobic interaction and gel filtration chromatography. The enzyme is a homodimer with subunit M r 39000. It had a specific activity of 500 mkat/kg of protein and was activated by the addition of Fe²⁺. The dehydrogenase converted 1 mol diene-diol and 1 mol NAD⁺ to 1 mol protocatechuic acid, 1 mol NADH and 1 mol CO₂. Apparent K _m-values of 43 μM (NAD⁺) and about 90 μM (diene-diol) were determined. The hydride ion was transferred to the si face of NAD⁺.     

The detection of hydroxyl radicals in vivo

Several indirect methods have been developed for the detection and quantification of highly reactive oxygen species (hROS), which may exist either as free hydroxyl radicals, bound “crypto” radicals or Fe(IV)-oxo species, in vivo. This review discusses the strengths and weaknesses associated with those most commonly used, which determine the hydroxylation of salicylate or phenylalanine. Chemical as well as biological arguments indicate that neither the hydroxylation of salicylate nor that of phenylalanine can guarantee an accurate hydroxyl radical quantitation in vivo. This is because not all hydroxylated product-species can be used for detection and the ratio of these species strongly depends on the chemical environment and on the reaction time. Furthermore, at least in the case of salicylate, the high concentrations of the chemical trap required (mM) are known to influence biological processes associated with oxidative stress.

Two, newer, alternative methods described, the 4-hydroxy benzoic acid (4-HBA) and the terephthalate (TA) assays, do not have these drawbacks. In each case reaction with hROS leads to only one hydroxylated product. Thus, from a chemical viewpoint, they should provide a better hROS quantitation. Further work is needed to assess any possible biological effects of the required millimolar (4-HBA) and micromolar (TA) concentrations of the chemical traps.