Adsorption of lignite-derived humic acids on coal-based mesoporous activated carbons

The adsorption by a coal-based mesoporous activated carbon of humic acids (HAs) isolated from two Polish lignites was studied. For comparison, a commercial Aldrich humic acid was also included into this study. The differences in chemical structure and functional groups of HAs were determined by elemental analysis and infrared spectroscopy DRIFT. Two activated carbons used differed in terms of mesopore volume, mesopore size distribution, and chemical properties of the surface. The kinetics of adsorption of HAs have been discussed using three kinetic models, i.e., the first-order Lagergren model, the pseudo-second-order model, and the intraparticle diffusion model. It was found that the adsorption of HAs from alkaline solution on mesoporous activated carbon proceeds according to the pseudo-second-order model. The correlation coefficients were close to 1. The intraparticle diffusion of HA molecules within the carbon particle was identified to be the rate-limiting step. Comparing the two activated carbons, the carbon with a higher volume of pores with widths of 10-50 nm showed a greater removal efficiency of HA. An increase in the Freundlich adsorption capacity with decreasing carbon content of HA was observed. Among the HAs studied, S-HA shows characteristics indicating the highest contribution of small-size fraction. The S-HA was removed by both activated carbons to the highest extent. The effect of pH solution on the adsorption of HA was examined over the range pH 5.4-12.2. It was found that the extent of adsorption decreased with decreasing pH of the solution.     

Interaction of water with the regenerated cellulose membrane studied by DSC

One to three endothermal peaks atributted to melting of bulk and interfacial water were observed by DSC in the regenerated cellulose — water system. The profiles of thermal effects depend on water content, time of conditioning, film pretreatment and the conditions applied during the preceding freezing-thawing cycles. The occurrence might be deduced of melting-crystallisation processes. A large amount of non-freezable strongly bounded water was also detected. Although cellulose absorbs water quickly after immersion, the structural changes consisting on ordering of polymer fraction occur during further conditioning due to increase in strength of water binding. Using the membranes in the separation module at 90°C causes weakening of these bonds. Differences between interaction of particular cellulose films with water can be detected during the first, the second and the third heating. This revised version was published online in July 2006 with corrections to the Cover Date.     

Kinetic and mechanistic studies on the reaction of nitric oxide with a water-soluble octa-anionic iron(III) porphyrin complex

The polyanionic water-soluble and non-mu-oxo-dimer-forming iron porphyrin iron(III) 5(4),10(4),15(4),20(4)-tetra-tert-butyl-5(2),5(6),15(2),15(6)-tetrakis[2,2-bis(carboxylato)ethyl]-5,10,15,20-tetraphenylporphyrin, (P(8-))Fe(III) (1), was synthesized as an octasodium salt by applying well-established porphyrin and organic chemistry procedures to bromomethylated precursor porphyrins and characterized by standard techniques such as UV-vis and (1)H NMR spectroscopy. A single pK(a1) value of 9.26 was determined for the deprotonation of coordinated water in (P(8-))Fe(III)(H(2)O)(2) (1-H(2)()O) present in aqueous solution at pH <9. The porphyrin complex reversibly binds NO in aqueous solution to give the mononitrosyl adduct, (P(8-))Fe(II)(NO(+))(L), where L = H(2)O or OH(-). The kinetics of the binding and release of NO was studied as a function of pH, temperature, and pressure by stopped-flow and laser flash photolysis techniques. The diaqua-ligated form of the porphyrin complex binds and releases NO according to a dissociative interchange mechanism based on the positive values of the activation parameters DeltaS() and DeltaV() for the "on" and "off" reactions. The rate constant k(on) = 6.2 x 10(4) M(-1) s(-1) (24 degrees C), determined for NO binding to the monohydroxo-ligated (P(8-))Fe(III)(OH) (1-OH) present in solution at pH >9, is markedly lower than the corresponding value measured for 1-H(2)O at lower pH (k(on) = 8.2 x 10(5) M(-1) s(-1), 24 degrees C, pH 7). The observed decrease in the reactivity is contradictory to that expected for the diaqua- and monohydroxo-ligated forms of the iron(III) complex and is accounted for in terms of a mechanistic changeover observed for 1-H(2)O and 1-OH in their reactions with NO. The mechanistic interpretation offered is further substantiated by the results of water-exchange studies performed on the polyanionic porphyrin complex as a function of pH, temperature, and pressure.     

Mechanistic studies on the binding of nitric oxide to a synthetic heme-thiolate complex relevant to cytochrome p450

The synthetic heme-thiolate complex (SR) in methanol binds nitric oxide (k(on) = (2.7 +/- 0.2) x10(6) M(-)(1) s(-)(1) at 25 degrees C) to form SR(NO). The binding of NO to the SR complex in a noncoordinating solvent, such as toluene, was found to be almost 3 orders of magnitude faster than that in methanol. The activation parameters DeltaH(), DeltaS(), and DeltaV() for the formation of SR(NO) in methanol are consistent with the operation of a limiting dissociative mechanism, dominated by dissociation of methanol in SR(MeOH). In the presence of an excess of NO, the formation of SR(NO) is followed by subsequent slower reactions. The substantially negative activation entropy and activation volume values found for the second observed reaction step support an associative mechanism which involves attack of a second NO molecule on the thiolate ligand in the initially formed SR(NO) complex. The following slower reactions are strongly accelerated by a large excess of NO or by the presence of NO(2)(-) in the SR/NO reaction mixture. They can be accounted for in terms of dynamic equilibria between higher nitrogen oxides (NO(x)()) and reactive SR species, which lead to the formation of a nitrosyl-nitrite complex of SR(Fe(II)) as the final product. This finding is clearly supported by laser flash photolysis studies on the SR/NO reaction mixture, which do not reveal simple NO photolabilization from SR(Fe(III))(NO), but rather involve the generation of at least three photoinduced intermediates decaying with different rate constants to the starting material. The species formed along the proposed reaction pathways were characterized by FTIR and EPR spectroscopy. The results are discussed in terms of their relevance for the biological function of cytochrome P450 enzymes and in context of results for the reaction of NO with imidazole- and thiolate-ligated iron(III) hemoproteins.     

Mechanistic information on the reversible binding of NO to selected iron(II) chelates from activation parameters

Mechanistic insight on the reversible binding of NO to Fe(II) chelate complexes as potential catalysts for the removal of NO from effluent gas streams has been obtained from the temperature and pressure parameters for the "on" and "off" reactions determined using a combination of flash photolysis and stopped-flow techniques. These parameters are correlated with those for water exchange reactions on the corresponding Fe(II) and Fe(III) chelate complexes, from which mechanistic conclusions are drawn. Small and positive Delta V(++) values are found for NO binding to and release from all the selected complexes, consistent with a dissociative interchange (I(d)) mechanism. The only exception in the series of studied complexes is the binding of NO to [Fe(II)(nta)(H(2)O)(2)](-). The negative volume of activation observed for this reaction supports the operation of an I(a) ligand substitution mechanism. The apparent mechanistic differences can be accounted for in terms of the electronic and structural features of the studied complexes. The results indicate that the aminocarboxylate chelates affect the rate and overall equilibrium constants, as well as the nature of the substitution mechanism by which NO coordinates to the selected complexes. There is, however, no simple correlation between the rate and activation parameters and the selected donor groups or overall charge on the iron(II) complexes.     

Molecular modeling of cytochrome P450 3A4

The three-dimensional structure of human cytochrome P450 3A4 was modeled based on crystallographic coordinates of four bacterial P450s: P450 BM-3, P450cam, P450terp, and P450eryF. The P450 3A4 sequence was aligned to those of the known proteins using a structure-based alignment of P450 BM-3, P450cam, P450terp, and P450eryF. The coordinates of the model were then calculated using a consensus strategy, and the final structure was optimized in the presence of water. The P450 3A4 model resembles P450 BM-3 the most, but the B helix is similar to that of P450eryF, which leads to an enlarged active site when compared with P450 BM-3, P450cam, and P450terp. The 3A4 residues equivalent to known substrate contact residues of the bacterial proteins and key residues of rat P450 2B1 are located in the active site or the substrate access channel. Docking of progesterone into the P450 3A4 model demonstrated that the substrate bound in a 6-orientation can interact with a number of active site residues, such as 114, 119, 301, 304, 305, 309, 370, 373, and 479, through hydrophobic interactions. The active site of the enzyme can also accommodate erythromycin, which, in addition to the residues listed for progesterone, also contacts residues 101, 104, 105, 214, 215, 217, 218, 374, and 478. The majority of 3A4 residues which interact with progesterone and/or erythromycin possess their equivalents in key residues of P450 2B enzymes, except for residues 297, 480 and 482, which do not contact either substrate in P450 3A4. The results from docking of progesterone and erythromycin into the enzyme model make it possible to pinpoint residues which may be important for 3A4 function and to target them for site-directed mutagenesis.     

Activities of Individual Ions From Infinite Dilution to Saturated Solutions

A new procedure, which provides a closer approximation for the junction potentials than the Henderson equation, is tested to reduce new emf data for the chloride ion in CsCl solutions and previously measured data for individual ions in aqueous solutions of KCl, NaCl, and NaBr. The liquid junction potential is calculated from numerical integration of its basic equation without assuming constant mobility or using concentrations instead of activities. The mean ionic activity coefficients of the salts, obtained from the activity coefficients of the individual ions, show good agreement with values reported in the literature. The activity coefficients of the individual chloride ion at 25°C in aqueous solutions of CsCl up to 3 molal and in KCl solutions were measured using a chloride ion-selective electrode. It has been confirmed that the activity of the chloride ion is equal to the activity of the cation in CsCl solutions and, contrary to the prediction of hydration theory, it is higher than the activity of the cation in aqueous KCl solutions. The New Hydration Theory has been developed to overcome the shortcomings of the older hydration theory and has been used to smooth the experimental activity coefficients of the individual ions in aqueous solutions and to extrapolate them up to the saturated solution.     

A detailed resonance Raman spectrum of Nickel(II)-substituted Pseudomonas aeruginosa azurin

Nickel(II) and cobalt(II) derivatives of the blue copper protein Pseudomonas aeruginosa azurin have been studied by resonance Raman (RR) spectroscopy at liquid-nitrogen temperatures. Vibrational assignments for the observed RR bands of Ni(II)-azurin have been made through a study of (62)Ni-substituted azurin. A comparison of Ni(II)-azurin RR spectra with those of the wild type (Cu-containing) protein showed Ni(II)-S(Cys) stretching vibrations, nu(Ni-S)(Cys), at substantially lower frequencies (approximately 360 versus approximately 400 cm(-1), respectively), indicating that the Ni(II)-S(Cys) bond is much weaker than the corresponding Cu(II)-S(Cys) bond. Resonance enhanced predominantly nu(Ni-N)(His) modes indicate that the metal-N(His) bond distances in the Ni(II) derivative are the same as those in native azurin. The vibrational data also confirm a tetrahedral disposition of ligands about the metal in Ni(II)-azurin found in the protein crystallographic structures. As expected, excitation profile measurements on Ni(II)-azurin show that the nu(Ni-S)(Cys) assignable modes give maxima at the 440-nm absorption band, which confirms a S(Cys) --> Ni(II) charge-transfer origin of the 440-nm electronic transition in Ni(II)-substituted azurin.     

Oxygenase‐Catalyzed Desymmetrization of N,N‐Dialkyl‐piperidine‐4‐carboxylic Acids

γ‐Butyrobetaine hydroxylase (BBOX) is a 2‐oxoglutarate dependent oxygenase that catalyzes the final hydroxylation step in the biosynthesis of carnitine. BBOX was shown to catalyze the oxidative desymmetrization of achiral N,N‐dialkyl piperidine‐4‐carboxylates to give products with two or three stereogenic centers.     

Electrospray ion-trap multistage mass spectrometry for characterisation of co-monomer compositional distribution of bacterial poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) at the molecular level

We report an electrospray ionisation multistage mass spectrometry (ESI-MSn) method that utilises molecular mass information for determination of sequence distribution and chemical structure of mass-selected macromolecules of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) biopolyester, PHBH. On the basis of ESI-MSn studies of PHBH oligomers obtained by partial alkaline depolymerisation of natural PHBH containing 13-14 mol% of hydroxyhexanoate (HH) units, the microstructure of this bacterial copolyester was assessed up to the level of 28 repeat units. The subtle structural details of the PHBH were evaluated based on sequencing of individual macromolecular ions thus showing the utility of this technique for the analysis of biological copolyester macromolecules. It was confirmed that both HH and hydroxybutyrate (HB) units of the PHBH copolymer are randomly distributed.