Pulse radiolysis of aqueous thiocyanate solution

The pulse radiolysis of N(2)O saturated aqueous solutions of KSCN was studied under neutral pH conditions. The observed optical absorption spectrum of the SCN(*) radical in solution is more complex than previously reported, but it is in good agreement with that measured in the gas phase. Kinetic traces at 330 and 472 nm corresponding to SCN(*) and (SCN)(2)(*-), respectively, were fit using a Monte Carlo simulation kinetic model. The rate coefficient for the oxidation of SCN(-) ions by OH radicals, an important reaction used in competition kinetics measurements, was found to be (1.4 +/- 0.1) x 10(10) M(-1) s(-1), about 30% higher than the normally accepted value. A detailed discussion of the reaction mechanism is presented.     

A pulse radiolysis study of free radicals formed by one-electron oxidation of the antimalarial drug pyronaridine

Free radicals from one-electron oxidation of the antimalarial drug pyronaridine have been studied by pulse radiolysis. The results show that pyronaridine is readily oxidised to an intermediate semi-iminoquine radical by inorganic and organic free radicals, including those derived from tryptophan and acetaminophen. The pyronaridine radical is rapidly reduced by both ascorbate and caffeic acid. The results indicate that the one-electron reduction potential of the pyronaridine radical at neutral pH lies between those of acetaminophen (707 mV) and caffeic acid (534 mV). The pyronaridine radical decays to produce the iminoquinone, detected by electrospray mass spectrometry, in a second-order process that density functional theory (DFT) calculations (UB3LYP/6-31+G*) suggest is a disproportionation reaction. Important calculated dimensions of pyronaridine, its phenoxyl and aminyl radical, as well as the iminoquinone, are presented. Electronic supplementary material  The online version of this article (doi:) contains supplementary material, which is available to authorized users.     

Electrodeposition of platinum nanoparticles in a room-temperature ionic liquid

The electrochemistry of the [PtCl(6)](2-)-[PtCl(4)](2-)-Pt redox system on a glassy carbon (GC) electrode in a room-temperature ionic liquid (RTIL) [i.e., N,N-diethyl-N-methyl-N-(2-methoxyethyl)ammonium tetrafluoroborate (DEMEBF(4))] has been examined. The two-step four-electron reduction of [PtCl(6)](2-) to Pt, i.e., reduction of [PtCl(6)](2-) to [PtCl(4)](2-) and further reduction of [PtCl(4)](2-) to Pt, occurs separately in this RTIL in contrast to the one-step four-electron reduction of [PtCl(6)](2-) to Pt in aqueous media. The cathodic and anodic peaks corresponding to the [PtCl(6)](2-)/[PtCl(4)](2-) redox couple were observed at ca. -1.1 and 0.6 V vs a Pt wire quasi-reference electrode, respectively, while those observed at -2.8 and -0.5 V were found to correspond to the [PtCl(4)](2-)/Pt redox couple. The disproportionation reaction of the two-electron reduction product of [PtCl(6)](2-) (i.e., [PtCl(4)](2-)) to [PtCl(6)](2-) and Pt metal was also found to occur significantly. The electrodeposition of Pt nanoparticles could be carried out on a GC electrode in DEMEBF(4) containing [PtCl(6)](2-) by holding the potential at -3.5 or -2.0 V. At -3.5 V, the four-electron reduction of [PtCl(6)](2-) to Pt can take place, while at -2.0 V the two-electron reduction of [PtCl(6)](2-) to [PtCl(4)](2-) occurs. The results obtained demonstrate that the electrodeposition of Pt at -3.5 V may occur via a series of reductions of [PtCl(6)](2-) to [PtCl(4)](2-) and further [PtCl(4)](2-) to Pt and at -2.0 V via a disproportionation reaction of [PtCl(4)](2-) to [PtCl(6)](2-) and Pt. Furthermore, the deposition potential of Pt nanoparticles was found to largely influence their size and morphology as well as the relative ratio of Pt(110) and Pt(100) crystalline orientation domains. The sizes of the Pt nanoparticles prepared by holding the electrode potential at -2.0 and -3.5 V are almost the same, in the range of ca. 1-2 nm. These small nanoparticles are "grown" to form bigger particles with different morphologies: In the case of the deposition at -2.0 V, the GC electrode surface is totally, relatively compactly covered with Pt particles of relatively uniform size of ca. 10-50 nm. On the other hand, in the case of the electrodeposition at -3.5 V, small particles of ca. 50-100 nm and the grown-up particles of ca. 100-200 nm cover the GC surface irregularly and coarsely. Interestingly, the Pt nanoparticles prepared by holding the potential at -2.0 and -3.5 V are relatively enriched in Pt(100) and Pt(110) facets, respectively.     

HEMATOPORPHYRIN PHOTOSENSITIZATION OF SERUM ALBUMIN and SUBTILISIN BPN'

—The photosensitized inactivation of subtilisin BPN' by free hematoporphyrin (HP) followed exponential kinetics with positive mechanistic tests for the involvement of singlet oxygen (¹O₂) as the principal intermediate. The photoinactivation quantum yield was 0.029 at 390 nm in oxygen-saturated, D₂O buffer at pH 7.0. The effects of HP binding were investigated for tryptophan oxidation in bovine serum albumin (BSA) and human serum albumin (HSA) at high protein:HP concentration ratios where the HP was > 97% complexed. The reaction kinetics were non-exponential and mimick a second-order process in the initial stages. The rate of HP photobleaching was 30-fold faster for complexed HP compared with free HP, which was shown to account for the observed kinetics. Mechanistic tests showed that ¹O₂ was the dominant photooxidizing intermediate of tryptophan residues and that it was not involved in the accompanying photobleaching of HP. The quantum yield for tryptophan oxidation in BSA was 0.11 at 390 nm in oxygen-saturated, D₂O buffer at pH 8.0. The reactivity of HSA was approximately 2-fold lower than BSA for equivalent conditions. Estimates of the reaction cross sections led to 3 Ų for the inactivation of subtilisin BPN' by ¹O₂ and 20 Ų for the oxidation of tryptophan in BSA.     

Oxidation of di- and tripeptides of tyrosine and valine mediated by singlet molecular oxygen, phosphate radicals and sulfate radicals.

Kinetics and mechanism of the oxidation of tyrosine (Tyr) and valine (Val) di- and tripeptides (Tyr-Val, Val-Tyr and Val-Tyr-Val) mediated by singlet molecular oxygen [O(2)((1)Delta(g))], phosphate (HPO(4)(*-) and PO(4)(*2-)) and sulfate (SO(4)(*-)) radicals was studied, employing time-resolved O(2)((1)Delta(g)) phosphorescence detection, polarographic determination of dissolved oxygen and flash photolysis. All the substrates were highly photooxidizable through a O(2)((1)Delta(g))-mediated mechanism. Calculated quotients between the overall and reactive rate constants for the quenching of O(2)((1)Delta(g)) by Tyr-derivatives (k(t)/k(r) values, accounting for the efficiency of the effective photooxidation) were 1.3 for Tyr, 1 for Tyr-Val, 2.8 for Val-Tyr and 1.5 for Val-Tyr-Val. The effect of pH on the kinetics of the photooxidative process confirms that the presence of the dissociated phenolate group of Tyr clearly dominates the O(2)((1)Delta(g)) quenching process. Products analysis by LC-MS indicates that the photooxidation of Tyr di- and tripeptides proceeds with the breakage of peptide bonds. The information obtained from the evolution of primary amino groups upon photosensitized irradiation is in concordance with these results. Absolute rate constants for the reactions of phosphate radicals (HPO(4)(*-) and PO(4)(*2-), generated by photolysis of the P(2)O(8)(4-) at different pH) and sulfate radicals (SO(4)(*-), produced by photolysis of the S(2)O(8)(2-)) with Tyr peptides indicate that for all the substrates, the observed tendency in the rate constants is: SO(4)(*-) > or = HPO(4)(*-) > or = PO(4)(*2-). Formation of the phenoxyl radical of tyrosine was detected as an intermediate involved in the oxidation of tyrosine by HPO(4)(*-).     

An electron paramagnetic resonance study of the influence of spermine on the photophysical reactions of tryptophan in aqueous solution at 77–200 K

The influence of the antioxidant spermine of the UV-induced formation of free radicals from tryptophan in frozen aqueous solutions was studied by electron paramagnetic resonance (EPR) instrumentation, and the stability of the radicals was investigated in the range 95–200 K. Without spermine, the tryptophan cation and neutral tryptophan radical were stabilized at 77 K; cations were formed by electron ejection from an excited singlet state, and neutral radicals by hydrogen donation from tryptophan in the triplet state. When present, spermine trapped the ejected photoelectrons; the rates of the two photoreactions of tryptophan were also influenced by spermine. Firstly, at low tryptophan concentrations, the yield of cations was reduced, due to diminished charge transfer from the excited singlet state to the solvation shell. Secondly, at high concentrations, minute additions of spermine enhanced intersystem crossing (which is quenched, in the absence of spermine, by dimerization) and, consequently, the yield of neutral radicals was increased. At 180 K, the electrons trapped by spermine were released and reacted with molecular oxygen to form the superoxide radical; at 190 K, the tryptophan radicals were thermally annealed.     

Photoionization of Indole, N-Methylindole and Tryptophan In Aqueous Solution upon Excitation at 193 nm

Abstract— The 193 nm photoionization of aqueous indole, A'-meth-ylindole and tryptophan–as a function of pH and under several saturating gas conditions–has been studied by laser photolysis using optical and conductometric detection methods. Monophotonic ionization leads to production of the cation radicals and hydrated electrons, the quantum yield of electron ejection is 0.3–0.4. The cation radicals have pK_a values of 4.5, <5 and 4.5 for indole, N -methylindole and tryptophan, respectively. Above these pH values, the cation radical deprotonate rapidly, having lifetimes of 1.0, ≅6 and 1.1 μs, respectively. Under N₂O, neutral indolyl radical production is accompanied by formation of an OH adduct radical (<1 μs). The conductivity results in Ar- and N₂O-saturated solution support the deprotonation mechanism and indicate that in the acidic pH range, the cation radical decays by release of protons with kinetics on the millisecond time scale.     

Kinetics and mechanisms of chlorine dioxide oxidation of tryptophan

The reactions of aqueous ClO2 (*) and tryptophan (Trp) are investigated by stopped-flow kinetics, and the products are identified by high-performance liquid chromatography (HPLC) coupled with electrospray ionization mass spectrometry and by ion chromatography. The rates of ClO2 (*) loss increase from pH 3 to 5, are essentially constant from pH 5 to 7, and increase from pH 7 to 10. The reactions are first-order in Trp with variable order in ClO2 (*). Below pH 5.0, the reactions are second- or mixed-order in [ClO2 (*)], depending on the chlorite concentration. Above pH 5.0, the reactions are first-order in [ClO2 (*)] in the absence of added chlorite. At pH 7.0, the Trp reaction with ClO2 (*) is first-order in each reactant with a second-order rate constant of 3.4 x 10(4) M(-1) s(-1) at 25.0 degrees C. In the proposed mechanism, the initial reaction is a one-electron oxidation to form a tryptophyl radical cation and chlorite ion. The radical cation deprotonates to form a neutral tryptophyl radical that combines rapidly with a second ClO 2 (*) to give an observable, short-lived adduct ( k obs = 48 s(-1)) with proposed C(H)-OClO bonding. This adduct decays to give HOCl in a three-electron oxidation. The overall reaction consumes two ClO2 (*) per Trp and forms ClO2- and HOCl. This corresponds to a four-electron oxidation. Decay of the tryptophyl-OClO adduct at pH 6.4 gives five initial products that are observed after 2 min and are separated by HPLC with elution times that vary from 4 to 17 min (with an eluent of 6.3% CH 3OH and 0.1% CH 3COOH). Each of these products is characterized by mass spectrometry and UV-vis spectroscopy. One initial product with a molecular weight of 236 decays within 47 min to yield the most stable product, N-formylkynurenine (NFK), which also has a molecular weight of 236. Other products also are observed and examined.     

Radiation induced decomposition of tryptophan in the presence of oxygen

Tryptophan decomposition in oxygenated aqueous solutions in neutral media was investigated by gamma and pulsed electron irradiation. By using pulse radiolysis it was found that 27% of tryptophan OH-adducts eliminate water. Tryptophan neutral radical, Trp, thus formed reacts rapidly with O^-•₂, k(Trp^•+O^-•₂) = (4.5±0.7) × 10⁹M^-1s^-1. The remaining tryptophan OH-adducts react with oxygen to give peroxy radicals which may eliminate O^-•₂, produce _N-formylkynurenine and disproportionate yielding organic peroxides. Peroxy radicals derived from tryptophan H-adducts regenerate tryptophan by the elimination of HO^•₂, and recombine with TrpH(OH)OO^• radicals producing organic peroxides.     

Electron transfer between guanosine radical and amino acids in aqueous solution. 1. Reduction of guanosine radical by tyrosine

As a model of chemical DNA repair, the reductive electron transfer from the aromatic amino acid tyrosine to the radical of the purine base guanosine monophosphate (GMP) was studied by time-resolved chemically induced dynamic nuclear polarization (CIDNP). The guanosyl radicals were photochemically generated in the quenching reaction of the triplet excited dye 2,2'-dipyridyl. Depending on the pH of the aqueous solution, four different guanosyl radicals were observed. The identification of the radicals was possible because of the high sensitivity of CIDNP to distinguish them through their ability or disability of participating in the degenerate electron hopping reaction with the diamagnetic molecules of guanosine monophosphate in the ground state. The CIDNP kinetics in this three-component system containing the dye, GMP, and N-acetyl tyrosine is strongly dependent on the efficiency of the electron-transfer reaction from tyrosine to the nucleotide radical. Quantitative analysis of the CIDNP kinetics obtained at different concentrations of the amino acid, together with the comparison with the CIDNP kinetics of the two-component systems (dipyridyl/tyrosine and dipyridyl/GMP) allowed for the determination of the rate constant ke of the reductive electron-transfer reaction for five pairs of reactants, with different protonation states depending on the pH: GH++*/TyrOH (pH 1.3), G+*/TyrOH (pH 2.9), G(-H)*/TyrOH (pH 7.5), G(-H)*/TyrO- (pH 11.3), and G(-2H)-*/TyrO- (pH 13.3). The rate constant ke varies from (7.1 +/- 3.0) x 10(8) M-1 s-1 (pH 1.3, 2.9) to less than 6 x 10(6) M-1 s-1 (pH 13.3).     

Structure-activity relationship of cyclic nitroxides as SOD mimics and scavengers of nitrogen dioxide and carbonate radicals

Synthetic nitroxide antioxidants attenuate oxidative damage in various experimental models. Their protective effect reportedly depends on ring size and ring substituents and is greater for nitroxides having lower oxidation potential. The present study focuses on the kinetics and mechanisms of the reactions of piperidine, pyrrolidine and oxazolidine nitroxides with HO2*/O2*-, *NO2 and CO3*- radicals, which are key intermediates in many inflammatory and degenerative diseases. It is demonstrated that nitroxides are the most efficient scavengers of *NO2 at physiological pH (k = (3-9) x 10(8) M(-1) s(-1)) and among the most effective metal-independent scavengers of CO3*- radicals (k = (2 - 6) x 10(8) M(-1) s(-1)). Their reactivity toward HO2*, though not toward *NO2 and CO3*-, depends on the nature of the ring side-chain and particularly on the ring-size. All nitroxide derivatives react slowly with O2*- and are relatively inefficient SOD mimics at physiological pH. Even piperidine nitroxides, having the highest SOD-like activity, demonstrate a catalytic activity of about 1000-fold lower than that of native SOD at pH 7.4. The present results do not indicate any correlation between the kinetics of HO2*/O2*-, *NO2 and CO3*- removal by nitroxides and their protective activity against biological oxidative stress and emphasize the importance of target-oriented nitroxides, i.e., interaction between the biological target and specific nitroxides.     

Kinetics and mechanism for reversible chloride transfer between mercury(II) and square-planar platinum(II) chloro ammine, aqua, and sulfoxide complexes. Stabilities, spectra, and reactivities of transient metal-metal bonded platinum-mercury adducts

The Hg2+aq- and HgCl+aq-assisted aquations of [PtCl4]2- (1), [PtCl3(H2O)]- (2), cis-[PtCl2(H2O)2] (3), trans-[PtCl2(H2O)2] (4), [PtCl(H2O)3]+ (5), [PtCl3Me2SO]- (6), trans-[PtCl2(H2O)Me2SO] (7), cis-[PtCl(H2O)2Me2SO]+ (8), trans-[PtCl(H2O)2M32SO]+ (9), trans-[PtCl2(NH3)2] (10), and cis-[PtCl2(NH3)2] (11) have been studied at 25.0 degrees C in a 1.00 M HClO4 medium buffered with chloride, using stopped-flow and conventional spectrophotometry. Saturation kinetics and instantaneous, large UV/vis spectral changes on mixing solutions of platinum complex and mercury are ascribed to formation of transient adducts between Hg2+ and several of the platinum complexes. Depending on the limiting rate constants, these adducts are observed for a few milliseconds to a few minutes. Thermodynamic and kinetics data together with the UV/vis spectral changes and DFT calculations indicate that their structures are characterized by axial coordination of Hg to Pt with remarkably short metal-metal bonds. Stability constants for the Hg2+ adducts with complexes 1-6, 10, and 11 are (2.1 +/- 0.4) x 10(4), (8 +/- 1) x 10(2), 94 +/- 6, 13 +/- 2, 5 +/- 2, 60 +/- 6, 387 +/- 2, and 190 +/- 3 M-1, respectively, whereas adduct formation with the sulfoxide complexes 7-9 is too weak to be observed. For analogous platinum(II) complexes, the stabilities of the Pt-Hg adducts increase in the order sulfoxide < aqua < ammine complex, reflecting a sensitivity to the pi-acid strength of the Pt ligands. Rate constants for chloride transfer from HgCl+ and HgCl2 to complexes 1-11 have been determined. Second-order rate constants for activation by Hg2+ are practically the same as those for activation by HgCl+ for each of the platinum complexes studied, yet resolved contributions for Hg2+ and HgCl+ reveal that the latter does not form dinuclear adducts of any significant stability. The overall experimental evidence is consistent with a mechanism in which the accumulated Pt(II)-Hg2+ adducts are not reactive intermediates along the reaction coordinate. The aquation process occurs via weaker Pt-Cl-Hg or Pt-Cl-HgCl bridged complexes.     

Photochemical reduction of cytochrome c by a 1,4,5,8-naphthalenediimide radical anion

Steady-state UV irradiation of aqueous solutions containing cytochrome c (cyt c) and N,N'-bis(2-phosphonoethyl)-1,4,5,8-naphthalenediimide (BPNDI), a water-soluble aromatic imide, resulted in the reduction of the heme iron from the Fe(III) to the Fe(II) oxidation state. The reaction kinetics were followed by the increase of the ferrocytochrome c absorbance band at 549 nm. The rate of the photochemical reaction was pH dependent, reaching its maximum values over the pH range 4-7. Addition of electrolyte (NaCl) at pH 5 resulted in a decrease in the reaction rate, as expected for reactions between oppositely charged species. Flash photolysis studies revealed that the actual reductant in the reaction was a photogenerated BPNDI radical anion, which transferred an electron to the cyt c heme iron. The participation of imide radicals in the process was confirmed by the ready reduction of cyt c by BPNDI radicals chemically generated with sodium dithionite.     

Free-radical-mediated oxidation of ascorbic acid by peroxomonosulphate

The kinetics of the oxidation of ascorbic acid (AH₂) by peroxomonosulphate (PMS) were determined in aqueous medium in acidic (pH 4.4), neutral (pH 7.0) and alkaline (pH 9.0) conditions over the temperature range 13-28°C. The reactions were found to obey total second-order kinetics, first-order each with respect to peroxomonosulphate and ascorbic acid concentration, obeying-d[AH₂]/dt = k ₂[PMS][AH₂]. Dehydroascorbic acid was detected as the product of the reaction. The stoichiometry of the reaction, [peroxomonosulphate]/[ascorbicacid] = 1 : 1, indicated the absence of self-decomposition of peroxomonosulphate. The influence of neutral salt (NaClO₄) was found to increase the reaction rate. Evidence for the formation of radical intermediates was obtained. A mechanism involving the formation of hydroxyl, sulphate and ascorbate free radicals as intermediates is proposed. The rate and activation parameters were evaluated to substantiate the mechanism proposed. A comparison is made with the corresponding reactions of the similar peroxides, S₂O₈ ^2- and P₂O₈ ^4-.     

Identification of oxidation products and free radicals of tryptophan by mass spectrometry

New oxidation products and free radicals derived from tryptophan (Trp) oxidation under Fenton reaction conditions were identified using mass spectrometry. After the oxidation of tryptophan using hydrogen peroxide and iron (II) system (Fenton reaction), mono- and dihydoxy tryptophans and N-formylkynurenine were identified using electrospray mass spectrometry (ES-MS) and ES-MS/MS. Besides these products, new products resulting from the reaction of tryptophan and oxidized tryptophan and 3-methyl indole derivatives were also identified. The 3-methyl indole derivatives resulted, most probably, from the oxidation process and not from in-source processes. A dimer formed by cross-linking between two Trp radicals (Trp-Trp), similar to the previously described tyrosine dimer was observed, as well as the corresponding monohydroxy-dimer (Trp-Trp-OH). Tandem mass spectrometry was used to identify the structures of these new oxidation products. Free radicals derived from tryptophan oxidation under Fenton reaction were detected using as spin trap the DMPO. The free radical species originated during the oxidation reaction formed stable adducts with the spin trap, and these adducts were identified by ES-MS. New adducts of oxidized tryptophan radicals, namely monohydroxy-tryptophan and dihydroxy-Trp dimer radicals, with one and two DMPO spin trap molecules where identified. Tandem mass spectrometry was used to confirm the proposed structure of the observed adducts.     

PHOTOCHEMICAL REACTION BETWEEN PROTEIN AND NUCLEIC ACIDS: PHOTOADDITION OF TRYPTOPHAN TO PYRIMIDINE BASES*1

Abstract— The photochemical interactions between tryptophan and nucleic acid bases were studied. When aqueous solutions of tryptophan were irradiated (Λ > 260 nm) at neutral pH in the presence of each of the nucleic acid bases, pyrimidine bases but not purine bases were altered. Air was found to decrease the rate of reaction. Two classes of photoproducts were isolated by thin layer and ion-exchange chromatography and partially characterized. One was the dihydro-pyrimidine forms of the base (see Reeve and Hopkins, 1979) and the other consisted of tryptophan-pyrimidine photoadducts. Four tryptophan-uracil and two tryptophan-thymine adducts each with a 1:1 molecular stochiometry were found. Spectroscopic measurements and a positive reaction with Ehrlich's reagent indicate that the indole nucleus remained intact, but that the pyrimidine base was reduced at the 5, 6 double bond. The absence of a positive ninhydrin reaction and the effect of pH on the quantum yield of the photoadduct formation indicated that the ionized a-amino acid group of tryptophan was involved in photoadduct formation. Indole derivatives lacking an a-amino group were also found to form photoadducts with pyrimidine bases. The experimental results are consistent with a reaction mechanism involving tryptophan excitation to the first excited singlet state as the initial event. Radical scavenging experiments indicate that tryptophan free radicals, formed by electron dissociation from the excited state, react with the ground state pyrimidine.     

Electron transfer between guanosine radicals and amino acids in aqueous solution. II. Reduction of guanosine radicals by tryptophan

The efficiency of the chemical pathway of DNA repair is studied by time-resolved chemically induced dynamic nuclear polarization (CIDNP) using the model system containing guanosyl base radicals, and tryptophan as the electron donor. Radicals were generated photochemically by pulsed laser irradiation of a solution containing the photosensitizer 2,2'-dipyridyl, guanosine-5'-monophosphate, and N-acetyl tryptophan. Depending on the pH of the aqueous solution, four protonation states of the guanosyl radical are formed via electron or hydrogen atom transfer to the triplet excited dye. The rate constants of electron transfer from the amino acid to the guanosyl radical were determined by quantitative analysis of the CIDNP kinetics, which is very sensitive to the efficiency of radical reactions in the bulk, and rate constants vary from (1.0 +/- 0.3) x 10(9) M(-1) s(-1) for the cation and dication radicals of the nucleotide to (1.2 +/- 0.3) x 10(7) M(-1) s(-1) for the radical in its anionic form. They were found to be higher than the corresponding values for electron transfer in the case of N-acetyl tyrosine as the reducing agent.     

Synthesis and spin-trapping properties of a new spirolactonyl nitrone

Spin trapping using electron paramagnetic resonance (EPR) spectroscopy is commonly employed for the identification of transient radicals in chemical and biological systems. A spirolactonyl-nitrone with rigid H-bond acceptor, 7-oxa-1-azaspiro[4.4]non-1-en-6-one 1-oxide, CPCOMPO, has been synthesized and characterized, and its spin-trapping properties were investigated. The rate of formation of CPCOMPO-O2H was determined using competition kinetics between the superoxide/hydroperoxyl radical (O2*-/HO2*) trapping by CPCOMPO and the spontaneous dismutation of this radical in aqueous media. The rate constant of 60 M-1.s-1 is the highest rate constant thus far observed at neutral pH for any nitrones using the kinetic method employed. Decay kinetics were also experimentally investigated for CPCOMPO-O2H. The effect of rigid H-bond acceptor on the stability of the CPCOMPO-O2H were computationally rationalized and compared to that of EMPO-O2H, which has flexible H-bond acceptor, and results show the need of a "loose" H-bond acceptor for improved adduct stability.     

Heterometallic platinum(II) compounds with β-aminoethylferrocenes: synthesis, electrochemical behaviour and anticancer activity

A new family of heterometallic compounds 3-6 containing ferrocenyl and platinum(II) centers has been synthesized by reaction of 1-β-aminoethylferrocene (1) and 1,1'-bis(β-aminoethyl)ferrocene (2) with Pt(II) precursors. Using K(2)[PtCl(4)] as the Pt(II) source, the cis-square-planar neutral compounds [Fe{η(5)-C(5)H(4)(CH(2))(2)NH(2)}(2)PtCl(2)] (3) and [{Fe(η(5)-C(5)H(4)(CH(2))(2)NH(2))(η(5)-C(5)H(5))}(2)PtCl(2)] (5) were obtained. Reaction of cis-[PtCl(2)(dmso)(2)] with 1 and 2 resulted in the displacement of dmso and chloride ligands from the platinum coordination sphere, affording the cationic and neutral compounds [Fe{η(5)-C(5)H(4)(CH(2))(2)NH(2)}(2)Pt(dmso)Cl]Cl (4) and [Fe(η(5)-C(5)H(4)(CH(2))(2)NH(2))(η(5)-C(5)H(5))Pt(dmso)Cl(2)] (6). Compounds 3-6 were thoroughly characterized using multinuclear ((1)H, (13)C, (195)Pt) NMR, IR spectroscopy, ESI mass spectrometry and elemental analysis. Single-crystal X-ray analysis of heterometallic 6 confirmed the cis geometry of the molecule and revealed that the platinum atom is held in a perfect square-planar geometry. The electrochemical behaviour of the heterometallic compounds 3-6, which has been examined by cyclic (CV) and square wave (SWV) voltammetries in dichloromethane and dmso solution, is characterized by the reversible one-electron oxidation of the ferrocene moieties. The results of the biological activity studies revealed that the organometallic complex 5 is active against all cell lines with GI(50) values in the range 1.7-2.3 μM. When compared to the standard anticancer drug cisplatin, heterotrimetallic 5, possessing two aminoethylferrocenyl units coordinated to the Pt(II) center, showed a greater activity profile in the colon cancer cell line. Cell cycle studies revealed that the new mixed compound exhibits a mechanism of action different to cisplatin.     

Determination of chloroplatinates by CE coupled to inductively coupled plasma sector field MS

In the present work the degradation of chloroplatinates emitted into the aquatic environment has been investigated in model studies. CE coupled to inductively coupled plasma sector field MS (ICP-SFMS) was employed as an analytical method of measurement. The CE-ICP-MS interface utilized the functional make-up flow design with a microconcentric nebulizer. [Pt(Cl(4))](2-) and [Pt(Cl(6))](2-) were separated within 5 min. During a measurement period of 6 h an excellent reproducibility of migration times (RSD 2.3%) could be achieved. The high sensitivity of ICP-SFMS resulted in an LOD of 80 ng/L platinum for the two compounds. External calibration using rhenium as internal standard was linear over three orders of magnitude. However, with external calibration a long-term drift of signal intensity was observed. In order to reduce the uncertainty of the obtained results, quantification of [PtCl(6)](2-) was performed for the first time by species-specific on-line isotope dilution MS using (194)[PtCl(6)](2-) as spike. The two different quantification strategies were compared in terms of their total combined uncertainty of measurement according to the EURACHEM guideline. The method was employed for monitoring the time-dependent degradation of [Pt(Cl(4))](2-) and [Pt(Cl(6))](2-) in water containing 0 and 2.8 mmol/L Cl(-) and river water. [Pt(Cl(6))](2-) was stable whereas [Pt(Cl(4))](2-) showed rapid degradation following pseudo first-order kinetics.