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PubMed2006

Sorption kinetics and chemical forms of Cd(II) sorbed by thiol-functionalized 2:1 clay minerals.

The interaction between Cd(II) in aqueous solution and two 2:1 expandable clay minerals (i.e., montmorillonite and vermiculite), showing different layer charge, was addressed via batch sorption experiments on powdered clay minerals both untreated and amino acid (cysteine) treated. Reaction products were characterized via X-ray powder diffraction (XRDP), chemical analysis (elemental analysis and atomic absorption spectrophotometry), thermal analysis combined with evolved gases mass spectrometry (TGA-MSEGA) and synchrotron-based X-ray absorption spectroscopy via extended X-ray absorption fine structure (EXAFS) characterization. Sorption isotherms for Cd(II) in presence of different substrates, shows that Cd(II) uptake depends both on Cd(II) starting concentration and the nature of the substrate. Thermal decomposition of Cd-cysteine treated clay minerals evidences the evolution of H(2)O, H(2)S, NO(2), SO(2), and N(2)O(3). These results are well consistent with XRDP data collected both at room and at increasing temperature and further stress the influence of the substrate, in particular cysteine, on the interlayer. EXAFS studies suggest that Cd(II) coordinates with oxygen atoms, to give monomer complexes or CdO molecules, either on the mineral surface and/or in the interlayer. For Cd-cysteine complexes EXAFS data agree with the existence of Cd-S clusters, thus suggesting a predominant role of the thiol group in the bonding of Cd with the amino acid.

Adsorption↗

PubMed2004

Equilibrium characterization of the As(III)-cysteine and the As(III)-glutathione systems in aqueous solution.

Some arsenic compounds were the first antimicrobial agents specifically synthesized for the treatment of infectious diseases such as syphilis and trypanosomiasis. More recently, arsenic trioxide has been shown to be efficient in the treatment of acute promyelocytic leukemia. The exact mechanism of action has not been elucidated yet, but it seems to be related to arsenic binding to vicinal thiol groups of regulatory proteins. Glutathione is the major intracellular thiol and plays important roles in the cellular defense and metabolism. This paper reports on a study of the interactions between arsenic(III) and either cysteine or glutathione in aqueous solution. The behavior observed for the As(III)-glutathione system is very similar to that of As(III)-cysteine. In both cases, the formation of two complexes in aqueous solution was evidenced by NMR and electronic spectroscopies and by potentiometry. The formation constants of the cysteine complexes [As(H(-1)Cys)(3)], log K = 29.84(6), and [As(H(-2)Cys)(OH)(2)](-), log K = 12.01(9), and of the glutathione complexes [As(H(-2)GS)(3)](3-), log K = 32.0(6), and [As(H(-3)GS)(OH)(2)](2-), log K = 10(3) were calculated from potentiometric and spectroscopic data. In both cases, the [As(HL)(3)] species, in which the amine groups are protonated, predominate from acidic to neutral media, and the [As(L)(OH)(2)] species appear in basic medium (the charges were omitted for the sake of simplicity). Spectroscopic data clearly show that the arsenite-binding site in both complexes is the sulfur atom of cysteine. In the [As(L)(OH)(2)] species, the coordination sphere is completed by two hydroxyl groups. In both cases, arsenic probably adopts a trigonal pyramidal geometry. Above pH 10, the formation of [As(OH)(2)O](-) excludes the thiolates from arsenic coordination sites. At physiological pH, almost 80% of the ligand is present as [As(HL)(3)].

Arsenic↗

PubMed2005

Zinc complexes with cyclic derivatives of alpha-ketoglutaric acid thiosemicarbazone: Synthesis, X-ray structures and DNA interactions.

Six new cyclic ligands derived from alpha-ketoglutaric acid thiosemicarbazone (H(3)ct) and their zinc complexes have been synthesized and characterized by analytical and spectroscopic (IR and NMR) studies. The X-ray structures of ligands Me-H(2)ct(C) (1), Allyl-H(2)ct(c) (3) and of complex [Zn(Me-Hct(C))(2)(OH(2))(2)].2H(2)O (7) have been determined. In complex (7) the zinc atom lies on a twofold axis and is surrounded in a tetrahedral coordination by two water molecules and two carboxylic oxygen donor atoms from the ligand. DNA titration in the UV-visible region and thermal denaturation have been employed to determine the details of DNA binding for the studied compounds. Studies of nuclease activity have also been performed with all our compounds through a gel electrophoresis experiment using plasmid pBR322 showing that no DNA breakings take place. Tests in vitro on human leukemia cell line U937 have been carried out on cell growth inhibition where solubility of the compounds allowed the experiments.

Cell Line, Tumor↗

PubMed2003

Fourteen protomers compose the oligomer III of the proton-rotor in spinach chloroplast ATP synthase.

Three fundamentally different chloroplast ATP synthase samples of increasing complexity were visualized by atomic force microscopy. The samples are distinguishable in respect to the isolation technique, the detergent employed, and the final subunit composition. The homo-oligomer III was isolated following SDS treatment of ATP synthase, the proton-turbine III+IV was obtained by blue-native electrophoresis, and complete CFO was isolated by anion exchange chromatography of NaSCN splitted ATP synthase. In all three ATP synthase subcomplexes 14 and only 14 circularly arranged subunits III composed the intact transmembrane rotor. Therefore, 14 protomers built the membrane-resident proton turbine. The observed stoichiometry of 14 is not a biochemical artifact or affected by natural growth variations of the spinach, as previously suggested. A correlation between the presence of subunit IV in the imaged sample and the appearance of a central protrusion in the narrower orifice of the oligomeric cylinder III14 has been observed. In contrast to current predictions, in chloroplast FO the subunit IV can be found inside the cylinder III14 and not at its periphery, at least in the reconstituted 2D arrays imaged.

Chloroplast Proton-Translocating ATPases↗

PubMed2005

Crystal structures of protein phosphatase-1 bound to motuporin and dihydromicrocystin-LA: elucidation of the mechanism of enzyme inhibition by cyanobacterial toxins.

The microcystins and nodularins are tumour promoting hepatotoxins that are responsible for global adverse human health effects and wildlife fatalities in countries where drinking water supplies contain cyanobacteria. The toxins function by inhibiting broad specificity Ser/Thr protein phosphatases in the host cells, thereby disrupting signal transduction pathways. A previous crystal structure of a microcystin bound to the catalytic subunit of protein phosphatase-1 (PP-1c) showed distinct changes in the active site region when compared with protein phosphatase-1 structures bound to other toxins. We have elucidated the crystal structures of the cyanotoxins, motuporin (nodularin-V) and dihydromicrocystin-LA bound to human protein phosphatase-1c (gamma isoform). The atomic structures of these complexes reveal the structural basis for inhibition of protein phosphatases by these toxins. Comparisons of the structures of the cyanobacterial toxin:phosphatase complexes explain the biochemical mechanism by which microcystins but not nodularins permanently modify their protein phosphatase targets by covalent addition to an active site cysteine residue.

Bacterial Toxins↗

PubMed2002

Mediator factor Med8p interacts with the hexokinase 2: implication in the glucose signalling pathway of Saccharomyces cerevisiae.

In the presence of glucose the protein hexokinase 2 (Hxk2p), normally resident in the cytosol, is translocated to the nucleus where it impairs the activation of transcription of the glucose-repressed genes HXK1, GLK1 and SUC2, and promotes the activation of transcription of the glucose-induced genes HXK2 and HXT1. Here, we demonstrate the involvement of an heptameric motif, named the MED8 site, in the direct binding of the mediator protein Med8p, either as a monomer or as a homodimer. Because this site was previously involved in the Hxk2p-dependent glucose-induced regulation of gene transcription, we tested whether Hxk2p interacts with Med8p. Our results show that Hxk2 and Med8 proteins are physically associated and that this Hxk2p-Med8p interaction is of physiological significance because both proteins have been found interacting together in a cluster with DNA fragments containing the MED8 site. We conclude that Hxk2p operates through the MED8 site, by interacting with Med8p, in the glucose signal transduction pathway of Saccharomyces cerevisiae.

DNA-Binding Proteins↗

PubMed1995

Bound to activate: conformational consequences of cyclin binding to CDK2.

The cyclin-dependent kinases (CDKs) are among the most highly regulated enzymes in the protein-kinase family. The crystal structures of cyclin A and the CDK2-cyclin A complex spectacularly reveal the atomic basis for regulation of these enzymes and provide a template for understanding the function and regulation of other members of the CDK family.

CDC2-CDC28 Kinases↗

PubMed1995

Calcium modulates the photoassembly of photosystem II (Mn)4-clusters by preventing ligation of nonfunctional high-valency states of manganese.

The requirement for Ca2+ in the Mn(2+)-dependent photoactivation of oxygen evolution was re-evaluated using 17 kDa/24 kDa-less photosystem II (PSII) membranes depleted of (Mn)4-clusters by NH2OH extraction. At optimum conditions (1 mM Mn2+/10 microM 2,6-dichlorphenolindophenol (DCIP)/20 mM Ca2+), the light-induced increase of oxygen-evolution activity, the increase of membrane-bound Mn, and the B-band thermoluminescence emission intensity occurred in parallel. The extent of recovery of the oxygen-evolution activity was equivalent to 88% and 66% of the activity shown by parent NaCl-extracted PSII membranes and by PSII membranes, respectively. Neither photodamage of primary electron transport nor photoligation of nonfunctional Mn > or = 3+ occurred. Analyses of the Ca2+ concentration dependence for the maximum recovery of oxygen evolution activity gave evidence for Ca(2+)-binding site(s) having Km values of approximately 38 and approximately 1300 microM. Illumination of membranes in the strict absence of Ca2+ resulted in large increases (up to 18 Mn/200 chlorophyll) of EDTA nonextractable, EPR silent, nonfunctional membrane-bound Mn > or = 3+ and small increases of oxygen-evolution capability, dependent on pH and concentrations of Mn2+ and DCIP. No photodamage of primary electron transport and only approximately 17% decrease of AT-band thermoluminescence occurred during the photoligation of the Mn > or = 3%. In the strict absence of Ca2+, significant recovery of oxygen-evolution activity was obtained under a limited set of conditions permitting photoligation of a limited abundance of the nonfunctional Mn > or = 3+. Small (NH2-OH, H2O2) as well as bulky external reductants readily reduced and dissociated the Mn > or = 3+ from the membranes. Reillumination of these membranes under optimal conditions for photoactivation (plus Ca2+) gave a high yield of (Mn)4-clusters and oxygen-evolution capability. Similarly, simple addition of Ca2+ to membranes containing nonfunctional Mn > or = 3+ followed by reillumination resulted in the conversion of Mn > or = 3+ to (Mn)4-clusters. It is argued that Ca2+ promotes the conformational change involved in the conversion of the Mn2+ mononuclear intermediate to the Mn(3+)-Mn2+ binuclear intermediate in the photoactivation mechanism, thereby permitting photoassembly of (Mn)4-clusters and preventing photo-inactivation by Mn > or = 3+ ions.

2,6-Dichloroindophenol↗

PubMed1984

Ligands for insulin receptor isolation.

Biotinylated insulins are bivalent molecules having the ability to bind to insulin receptors on the one hand and to "avidins" on the other. In order to be useful as ligands for insulin receptor isolation, biotinylated insulins must be developed that have the capacity to bind simultaneously to both and insulin receptor. The present investigation addresses this problem. A series of biotinylated and dethiobiotinylated insulins has been prepared in which the distance between the biotin carboxyl group and the insulin varies from 7 to 20 atoms. These compounds form complexes with succinoylavidin. The dissociation rates (K-1) of these complexes have been determined from the [14C]biotin exchange assay. The dissociation kinetics of most of these complexes are biphasic, and the kinetic constants reported are those corresponding to the slow rate. Ligands containing dethiobiotin dissociate more rapidly than the corresponding biotin derivatives. The interposition of a spacer arm substantially decreases the rate of dissociation. The [14C]biotin exchange assay could not be used with streptavidin complexes of the above ligand since biotin dissociates more rapidly from streptavidin than from succinoylavidin. However, the relative dissociation rates of a series of ligands could be determined and were as follows: 6-(dethiobiotinylamido)-hexanoic acid greater than dethiobiotinyl-A1-insulin greater than biotinylinsulin greater than biotinyl-A1-insulin greater than biotinyl-A2-insulin. Dethiobiotin and its amide failed to form complexes with streptavidin. The affinity of the ligands for insulin receptors was determined by measuring their ability to stimulate 14CO2 formation from [1-14C]glucose in rat epididymal adipocytes.(ABSTRACT TRUNCATED AT 250 WORDS)

Adipose Tissue↗

PubMed1975

Optical and magnetic resonance studies of formate binding to horse liver catalase and sperm whale myoglobin.

The binding of formate ion, a substrate for the peroxidatic reaction of catalase, has been investigated by magnetic resonance techniques. Comparative studies of formate binding to ferric myoglobin have also been performed. The nuclear magnetic relaxation (NMR) rate of formate and water protons is enhanced by the presence of ferric horse liver catalase. The enhancement is not changed significantly by the addition of cyanide, indicating that water and formate are still bound in the presence of cyanide. Formate proton to heme iron distances determined by magnetic resonance techniques indicate that formate does not directly bind to the heme iron of catalase or myoglobin but to the globin, and NMR relaxation occurs as a result of outersphere mechanisms. Evidence that water forms an innersphere complex with the iron atom of the catalase heme is presented. In similar experiments with ferric myoglobin, the addition of cyanide caused a large decrease in the enhancement of the proton relaxation rate of both formate and water, indicating the displacement of water and formate from the heme and the vicinity of the heme, respectively. Broad, high-spin, ferric ion electron paramagnetic resonance absorptions of catalase and myoglobin at room temperature obtained in the presence and absence of formate show that formate does not alter appreciably the heme environment of catalase or myoglobin or the spin state of the heme iron. Studies on the binding of formate to catalase as monitored by changes in the heme absorption spectrum in the visible region show one-to-one stoichiometry with heme concentration. However, the small changes observed in the visible region of the optical spectrum on addition of formate ion are attributed to a secondary effect of formate on the heme environment, rather than direct binding of formate to the heme moiety.

Animals↗

PubMed2005

Solution structure of zinc- and calcium-bound rat S100B as determined by nuclear magnetic resonance spectroscopy.

The EF-hand calcium-binding protein S100B also binds one zinc ion per subunit with a relatively high affinity (K(d) approximately 90 nM) [Wilder et al., (2003) Biochemistry 42, 13410-13421]. In this study, the structural characterization of zinc binding to calcium-loaded S100B was examined using high-resolution NMR techniques, including structural characterization of this complex in solution at atomic resolution. As with other S100 protein structures, the quaternary structure of Zn(2+)-Ca(2+)-bound S100B was found to be dimeric with helices H1, H1', H4, and H4' forming an X-type four-helix bundle at the dimer interface. NMR data together with mutational analyses are consistent with Zn(2+) coordination arising from His-15 and His-25 of one S100B subunit and from His-85 and Glu-89 of the other subunit. The addition of Zn(2+) was also found to extend helices H4 and H4' three to four residues similar to what was previously observed with the binding of target proteins to S100B. Furthermore, a kink in helix 4 was observed in Zn(2+)-Ca(2+)-bound S100B that is not in Ca(2+)-bound S100B. These structural changes upon Zn(2+)-binding could explain the 5-fold increase in affinity that Zn(2+)-Ca(2+)-bound S100B has for peptide targets such as the TRTK peptide versus Ca(2+)-bound S100B. There are also changes in the relative positioning of the two EF-hand calcium-binding domains and the respective helices comprising these EF-hands. Changes in conformation such as these could contribute to the order of magnitude higher affinity that S100B has for calcium in the presence of Zn(2+).

Animals↗

PubMed1997

Analysis of the reaction coordinate of photosynthetic water oxidation by kinetic measurements of 355 nm absorption changes at different temperatures in photosystem II preparations suspended in either H2O or D2O.

Flash-induced absorption changes at 355 nm were measured at different temperatures within the range of 2 degrees C </= theta </= 25 degrees C in dark-adapted PS II core complexes from spinach [O2 evolution rate: 1500 +/- 100 micromol of O2 (mg of Chl)-1 h-1] that were dissolved either in H2O- or in D2O-containing buffer. Comparative measurements were performed at 20 degrees C in H2O- or D2O-containing suspensions of PS II membrane fragments [O2 evolution rate: 600 +/- 40 micromol of O2 (mg of Chl)-1 h-1]. The results obtained reveal the following: (a) The activation energies of the individual redox steps in the water oxidizing complex (WOC) are dependent on the redox state Si with EA(S1-->S2) = 14 kJ/mol, EA(S2-->S3) = 35 kJ/mol, and EA(S3-->-->S0 + O2) = 21 kJ/mol for theta > 11 degrees C, 67 kJ/mol for theta < 11 degrees C in PS II core complexes dissolved in H2O; (b) replacement of exchangeable protons by deuterons causes only minor changes (</=15%) of the activation energies; and (c) the rate constants of these reactions in PS II core complexes are characterized by H/D isotope ratios, ki(H)/ki(D), of 1.6, 2.3, and 1.5 for the transitions S1 --> S2, S2 --> S3, and S3 -->--> S0 + O2, respectively. The corresponding values of PS II membrane fragments are 1.3, 1.3, and 1. 4. Based on these results and corresponding EA data reported in the literature for PS II membrane fragments from spinach [Renger, G., & Hanssum, B. (1992) FEBS Lett. 299, 28-32] and PS II particles from the thermophilic cyanobacterium Synechococcus vulcanus Copeland [Koike, H., Hanssum, B., Inoue, Y., & Renger, G. (1987) Biochim. Biophys. Acta 893, 524-533], the reaction coordinate of the redox sequence in the WOC is inferred to be almost invariant to the evolutionary development from cyanobacteria to higher plants. Furthermore, the rather high activation energy of the S2 --> S3 transition provides evidence for a significant structural change coupled with this reaction. Implications for the mechanism of photosynthetic water oxidation are discussed.

Deuterium Oxide↗

PubMed1997

The photosynthetic oxygen evolving complex requires chloride for its redox state S2-->S3 and S3-->S0 transitions but not for S0-->S1 or S1-->S2 transitions.

The Cl- requirement in the redox cycle of the oxygen-evolving complex (OEC) was determined by measurements of flash-induced UV absorbance changes in Cl(-)-depleted and Cl(-)-reconstituted photosystem II membranes. On the first flash after dark adaptation the spectrum and amplitude of those changes, known to reflect the oxidation of MnIII to MnIV on the S1-->S2 transition, were the same in the presence or absence of Cl-. On the second and later flashes, however, absorbance changes in Cl(-)-depleted samples revealed only electron transfer from tyrosine to quinone which reversed slowly in the dark by charge recombination and did not produce the S3-state. A rapid method was developed to remove Cl- after producing the S3-state by two flashes. The lifetime of the S3-state was found to be unaffected by Cl(-)-depletion, in contrast to the 20-fold stabilization of the S2 lifetime by Cl- removal, and the Cl(-)-depleted S3-state did not proceed to S0 on flash illumination. However, when the same Cl(-)-depletion procedure was applied after producing the S0-state by three flashes, further advance to S2 by two additional flashes was not impaired by the absence of Cl-. The requirement for Cl- only on the S2-->S3 and S3-->S0 transitions can be rationalized by the hypothesis that Cl- is required for electron transfer between manganese ions within the oxygen-evolving complex.

Chlorides↗

PubMed1998

Relationship between activity, D1 loss, and Mn binding in photoinhibition of photosystem II.

Photoinhibition of photosystem II (PSII) activity and loss of the D1 reaction center protein were studied in PSII-enriched membrane fragments in which the water-splitting complex was inhibited by depletion of either calcium or chloride or by removing manganese. The Ca2+-depleted PSII was found to be the least susceptible to inhibition by light as reported previously (Krieger, A., and Rutherford, A. W. (1997) Biochim. Biophys. Acta 1319, 91-98). This different susceptibility to light was not reflected in the extent of D1 protein loss. In Mn-depleted PSII the loss of activity and the loss of the D1 protein were correlated, while in Cl-- and Ca2+-depleted PSII, there was very little loss of the D1 protein. The production of free radicals and singlet oxygen was measured by EPR spin-trapping techniques in the different samples. 1O2 and carbon-centered radicals could be detected after photoinhibition of active PSII, while hydroxyl radical formation dominated in all of the other samples. In addition, photoinhibition of PSII was investigated in which the functional Mn cluster was reconstituted (i. e., photoactivated). As expected this led to a protection against photoinhibition. When the photoactivation procedure was done in the absence of Ca2+ no activity was obtained although a nonfunctional Mn cluster was formed. Despite the lack of activity the binding of Mn partially protected against the loss of D1. These data demonstrate that, during photoinhibition, the extent of D1 loss is neither affected by the water-splitting activity of the sample nor correlated to the kinetics of PSII activity loss. D1 loss seems to be independent of the chemical nature of the reactive oxygen species formed during photoinhibition and seems to occur only in the absence of Mn. It is proposed that Mn binding protects against D1 loss by maintaining a protein structure which is not accessible to cleavage.

Binding Sites↗

PubMedDate not supplied

Virtual screening for SARS-CoV protease based on KZ7088 pharmacophore points.

Pharmacophore modeling can provide valuable insight into ligand-receptor interactions. It can also be used in 3D (dimensional) database searching for potentially finding biologically active compounds and providing new research ideas and directions for drug-discovery projects. To stimulate the structure-based drug design against SARS (severe acute respiratory syndrome), a pharmacophore search was conducted over 3.6 millions of compounds based on the atomic coordinates of the complex obtained by docking KZ7088 (a derivative of AG7088) to SARS CoV M(pro) (coronavirus main proteinase), as reportedly recently (Chou, K. C.; Wei, D. Q.; Zhong, W. Z. Biochem. Biophys. Res. Commun. 2003, 308, 148-151). It has been found that, of the 3.6 millions of compounds screened, 0.07% are with the score satisfying five of the six pharmacophore points. Moreover, each of the hit compounds has been evaluated for druggability according to 13 metrics based on physical, chemical, and structural properties. Of the 0.07% compounds thus retrieved, 17% have a perfect score of 1.0; while 23% with one druggable rule violation, 13% two violations, and 47% more than two violations. If the criterion for druggability is set at a maximum allowance of two rule violations, we obtain that only about 0.03% of the compounds screened are worthy of further tests by experiments. These findings will significantly narrow down the search scope for potential compounds, saving substantial time and money. Finally, the featured templates derived from the current study will also be very useful for guiding the design and synthesis of effective drugs for SARS therapy.

Coronavirus 3C Proteases↗

PubMedDate not supplied

Probing fragment complementation by rigid-body docking: in silico reconstitution of calbindin D9k.

Fragment complementation is gaining an increasing impact as a nonperturbing method to probe noncovalent interactions within protein supersecondary structures. In this study, the fast Fourier transform rigid-body docking algorithm ZDOCK has been employed for in silico reconstitution of the calcium binding protein calbindin D9k, from its two EF-hands subdomains, namely, EF1 (residues 1-43) and EF2 (residues 44-75). The EF1 fragment has been used both in its wild type and in nine mutant forms, in line with in vitro experiments. Consistent with in vitro data, ZDOCK reconstituted the proper fold of wild-type and mutated calbindin, locating the nativelike structures (i.e., holding a root-mean-square deviation < 1 A with respect to the X-ray structure) among the first 10 top-scored solutions out of 4000. Moreover, the three independent in silico reconstitutions of wild-type calbindin ranked a nativelike structure at the top of the output list, that is, the best scored one. The algorithm has been also successfully challenged in reconstituting the EF2 homodimer from two identical copies of the monomer. Furthermore, quantitative models consisting of linear correlations between thermodynamic data and ZDOCK scores were built, providing a tested tool for very fast in silico predictions of the free energy of association of protein-protein complexes solved at the atomic level and known to not undergo significant conformational changes upon binding.

Calbindins↗

PubMed2001

Sorption and desorption behavior of organotin compounds in sediment-pore water systems.

Sediments contaminated with organotin compounds (OTs), in particular triorganotins (TOTs), are abundant in areas with high shipping activities. To assess the possible remobilization of these highly toxic compounds from such sediments, a profound understanding of their sorption/desorption behavior is necessary. In this work the extent and reversibility of sorption of OTs to sediments has been investigated using contaminated freshwater harbor sediments and two certified OT containing marine sediments. Experiments conducted with perdeuterated OTs showed that sorption of OTs to sediments is a fast and reversible process involving primarily particulate organic matter (POM) constituents as sorbents. The organic carbon-normalized sediment-water distribution ratios (DOC, expressed in L/kgOC) determined in the laboratory were consistent with in-situ DOCs obtained from OT concentrations measured in sediment and pore water samples from two dated sediment cores. For both butyl- and phenyltin compounds the log DOC values were in the range of 4.7-6.1, and the following sequence was observed: DOC (tri-OT) > or = DOC (di-OT) > or = DOC (mono-OT). However, the differences were much less pronounced than would have been expected for hydrophobic partitioning of the corresponding compounds into POM. These results support our hypothesis from earlier work with dissolved humic acids that OT sorption to sediments occurs primarily by reversible formation of (innerspere) complexes between the tin atom and carboxylate and phenolate ligands present in POM. Because of the high DOC values (i.e. log DOC > or = 4) the diffusion of OTs from deeper sediments to the surface will be rather slow, and thus a major release from undisturbed sediments is not expected. However, because OTs readily desorb, any resuspension of contaminated sediments (e.g., by the tide, storms or dredging activities) will lead to enhanced OT concentrations in the overlaying water column. Furthermore, in contrastto polycyclic aromatic hydrocarbons (PAH) where large fractions may be tightly bound (in)to soot or other carbonaceous materials, OTs will be more readily bioavailable due to the fast and reversible sorption/desorption behavior.

Absorption↗

PubMed2000

Ligand macrocycle structural effects on copper-dioxygen reactivity.

With the goal of understanding how the nature of the tridentate macrocyclic supporting ligand influences the relative stability of isomeric mu-eta 2:eta 2-peroxo- and bis(mu-oxo)dicopper complexes, a comparative study was undertaken of the O2 reactivity of Cu(I) compounds supported by the 10- and 12-membered macrocycles, 1,4,7-R3-1,4,7-triazacyclodecane (R3TACD; R = Me, Bn, iPr) and 1,5,9-triisopropyl-1,5,9-triazacyclododecane (iPr3TACDD). While the 3-coordinate complex [(iPr3TACDD)Cu]SbF6 was unreactive with O2, oxygenation of [(R3TACD)Cu(CH3CN)]X (R = Me or Bn; X = ClO4- or SbF6-) at -80 degrees C yielded bis(mu-oxo) species [(R3TACD)2Cu2(mu O)2]X2 as revealed by UV-vis and resonance Raman spectroscopy. Interestingly, unlike the previously reported system supported by 1,4,7-triisopropyl-1,4,7-triazacyclononane (iPr3TACN), which yielded interconverting mixtures of peroxo and bis(mu-oxo) compounds (Cahoy, J.; Holland, P. L.; Tolman, W. B. Inorg. Chem. 1999, 38, 2161), low-temperature oxygenation of [(iPr3TACD)Cu(CH3CN)]SbF6 in a variety of solvents cleanly yielded a mu-eta 2:eta 2-peroxo product, with no trace of the bis(mu-oxo) isomer. The peroxo complex was characterized by UV-vis and resonance Raman spectroscopy, as well as an X-ray crystal structure (albeit of marginal quality due to disorder problems). Intramolecular attack at the alpha C-H bonds of the substituents was indicated as the primary decomposition pathway of the oxygenated compounds through examination of the decay kinetics and the reaction products, which included bis(mu-hydroxo)- and mu-carbonato-dicopper complexes that were characterized by X-ray diffraction. A rationale for the varying results of the oxygenation reactions was provided by analysis of (a) the X-ray crystal structures and electrochemical behavior of the Cu(I) precursors and (b) the results of theoretical calculations of the complete oxygenated complexes, including all ligand atoms, using combined quantum chemical/molecular mechanics (integrated molecular orbital molecular mechanics, IMOMM) methods. The size of the ligand substituents was shown to be a key factor in controlling the relative stabilities of the peroxo and bis(mu-oxo) forms, and the nature of this influence was shown by both theory and experiment to depend on the ligand macrocycle ring size.

Copper↗