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PubMed1991

Bivalent ligand dissociation kinetics from receptor-bound immunoglobulin E: evidence for a time-dependent increase in ligand rebinding at the cell surface.

The bivalent ligand N,N'-bis[[epsilon-[(2,4- dinitrophenyl)amino]caproyl]-L-tyrosyl]cystine [(DCT)2-Cys] binds and cross-links anti-dinitrophenyl (DNP) immunoglobulin E (IgE)-receptor complexes on the cell surface of rat basophilic leukemia cells. The rate of dissociation of this bound ligand was monitored by using a fluorescence method under two different conditions. In one case the monovalent ligand DCT was added in large excess to prevent the dissociating ligand from rebinding to unoccupied antibody combining sites. Under these conditions, dissociation of the bivalent ligand from IgE-sensitized cells proceeds to completion with kinetics that are well described by two rate constants that are independent of the time of preincubation of the bivalent ligand with the cells. In the second case, dissociation of (DCT)2-Cys from cell-bound anti-DNP IgE was monitored in the presence of a large excess of anti-DNP IgE in solution that acts as a sink to absorb the dissociated ligand. Under these conditions, the bivalent ligand becomes more resistant to dissociation as the preincubation time of the bivalent ligand with the cells is increased. An increasing fraction of the bound ligand does not dissociate on a measurable time scale in the presence of this sink. The results indicate that cell-associated IgE-receptor complexes undergo a time-dependent change that facilitates the reformation of the cross-linked state when one end of the ligand dissociates to break up the existing cross-link. The possible physical basis and functional implications of these results are discussed.

Animals↗
PubMed1984

Light-scattering investigation of the subunit structure and dissociation of Helix pomatia hemocyanin. Effects of salts and ureas.

The effects of various salts of the Hofmeister and aliphatic acid salt series and hydrophobic reagents of the urea series on the subunit structure and the dissociation of Helix pomatia alpha-hemocyanin were investigated by employing light-scattering molecular weight methods. In moderate ranges of salt concentrations [0-1.0 M NaClO4, NaSCN, NaI, and guanidinium chloride (GdmCl) and 0-2.0 M NaBr], the dissociation reaction is essentially a two-step process characterized by the dissociation of whole hemocyanin molecules dissociating to half-molecules of decamers followed by the dissociation of the half-molecules to five dimeric fragments. The effectiveness of the salts and relative ineffectiveness of the ureas and GdmCl as dissociating agents in the first step of the dissociation reaction suggest that the stabilization of the contact areas between half-molecules in solution is largely a nonhydrophobic energy process involving polar and ionic interactions. Hydrophobic forces appear to be important, however, for stabilization of the half-molecules through side to side contacts of the five dimeric units that make up each half-molecule. The analysis of our dissociation data by use of equations derived in our previous studies [Herskovits, T. T., & Harrington, J.P. (1975) Biochemistry 14, 4964-4971] gave apparent estimates of amino acid groups of about 60-150 for each of the contact areas between the cylindrically shaped half-molecules and 30-60 for each of the dimers in the half-molecules themselves.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1984

Differential dissociation of histone tails from core chromatin.

The dissociation of the trypsin-sensitive basic tails of the core histones in core chromatin has been followed as a function of [NaCl] using proton NMR spectroscopy. The tails dissociate in a highly cooperative all or none manner over the salt concentration range 0.2-0.6 M, that is, below the salt concentration required to dissociate the complete molecule. Assuming that each basic tail dissociates independently, the total number of salt linkages involved in binding the tails to DNA is 103. This equals the number of basic side chains in the tails of an octamer. The standard free energy of dissociation, delta G degree, in 1 M NaCl at 297 K is 3.6 kcal/mol. Temperature had no effect on the extent of dissociation up to 45 degrees C. However, between 45 and 65 degrees C, where the premelting transition in the core chromatin occurs, the tails dissociated completely. Dissociation of the tails was associated with a conformational transition in the DNA consistent with loss of supercoiling. From this, and the results of a previous study, it can be shown that the structured, trypsin-resistant domain of each core histone octamer makes 100 salt linkages to DNA. Thus, in 10 mM salt, each core octamer makes a total of 203 salt linkages to DNA.

Animals↗
PubMed1978

Arginine decarboxylase from Escherichia coli B: mechanism of dissociation from the decamer to the dimer.

The mechanism by which arginine decarboxylase dissociates from a decamer to a dimer has been examined by allowing a sulfhydryl group, available in the dimer but not the decamer, to react with 5,5'-dithiobis(2-nitrobenzoic acid). Initial rates of dissociation were obtained by following the resulting increase in absorbance at 412 nm in a stopped-flow spectrophotometer. The rate of dissociation increases linearly with the protein concentration and reaches a maximum as a function of the concentrations of 5,5'-dithiobis(2-nitrobenzoic acid), Na+, and 1/[H+]. Experiments in which the rate of dissociation was measured while one reagent was varied at fixed levels of a second indicate that dissociation requires three events: binding of one Na+ ion, dissociation of one proton, and the irreversible dissociation of subunits, in that order. The results also show that the decamer dissociates in stages rather than all at once. The activation energy for the overall process is 16 kcal/mol.

Arginine↗
PubMed1978

Mechanisms and rate equations for dissociating systems.

The results presented in the previous paper (Boeker, E.A. (1978), Biochemistry 17 (preceding paper in this issue) indicate that the dissociation of the decamer of arginine decarboxylase of Escherichia coli B is enhanced by Na+ and retarded by H+. In this system, substances which increase the rate of dissociation can be treated kinetically either as substrates or activators, and substances which retard dissociation can be treated as products or inhibitors. In addition, the events needed for dissociation can occur in an ordered or a random sequence, and the dissociation itself, from a decamer to five dimers, can be a sequential or a concerted process. In order to provide a framework for the experimental results, mechanisms for the dissociation of arginine decarboxylase that take all of these factors into account are described. In addition, it is shown that the usual methods of steady-state kinetics can be applied to these systems when true initial rates are measured; rate equations are presented for each mechanism. The results can be used for any dissociating of three or more subunits and will describe the dissociation of a dimer under certain conditions.

Arginine↗
PubMed1977

Studies on native ribosomal subunits from rat liver. Purification and characterization of a ribosome dissociation factor.

A population of free, native ribosomal 40S subunits, that do not react with 60S subunits to form 80S ribosomes, has been identified in the postmicrosomal fraction of rat liver homogenates. A protein (IF-3) has been purified from high salt (0.88 M KCI) extracts of native 40S subunits by gradient centrifugation and by ammonium sulfate fractionation; it prevents the reassociation of subunits and to a limited extent dissociates ribosomes to subunits. The activity is measured by ultracentrifugation of the reaction products on linear sucrose gradients, or with an assay developed in this laboratory that couples dissociation with the 60S-specific peptidyltransferase reaction; the latter procedure measures the amount of 60S subunits released from ribosomes or remaining in incubations in the presence of IF-3. Dissociation factor activity is recovered from most of the particles that are resolved by zonal centrifugation of the total "native subunits" obtained from the postmicrosomal fraction; the highest concentration of IF-3, however, appears to be associated with native 40S subunits. The purified dissociation factor IF-3 is composed of about ten polypeptides and the molecular weight is estimated to be between 500 000 and 700 000, on the basis of glycerol and cesium chloride gradient centrifugation. When purified 40S subunits react with IF-3 or when 80S ribosomes are dissociated by IF-3, a product is formed which is dependent on the concentration of the protein factor and has the characteristics of a 40SIF-3 complex; centrifugation of the complex on sucrose and cesium chloride gradients suggests that the complex consists of 1 equiv of each of the two components. Although dissociation factor IF-3 appears to react in a specific manner with free or ribosome-associated 40S subunits, the reaction with subunits differs in several respects from that with ribosomes. The dissociation factor also appears to interact with 60S subunits but multiple complexes are formed, some with more than 1 IF-3 equiv per 60S particle. The IF-3 converts 40S dimers (55S particles) to the 40S-IF-3 complex and dissociates free, native 80S particles present in the postmicrosomal fraction, but it does not affect polysome-associated ribosomes engaged in protein synthesis.

Animals↗
PubMed1976

Kinetics of deoxyhemoglobin subunit dissociation determined by haptoglobin binding: estimation of the equilibrium constant from forward and reverse rates.

Deoxyhemoglobin tetramers dissociate into dimers very slowly, with half-times on the order of several hours. It is demonstrated that absorbance changes in the Soret region which accompany this dissociation and persist upon binding of haptoglobin 1-1 to the dissociated dimers can be used for accurate kinetic determinations over the necessarily long periods required for study. This method of study for the slow reactions depends upon long-term spectral integrity of the reaction mixtures and upon accurate measurement. The variation in rate constants determined by this procedure has been correlated with variations in structural constraints at the dimer-dimer contact region. In the presence of 2,3-diphosphoglycerate the rate constant is decreased, consistent with the role of this effector in binding to both beta chains and stabilizing the constrained deoxy tetramer against dissociation into alphabeta dimers. With hemoglobin specifically modified (des-Arg-141alpha) to eliminate half the constraining salt links within the dimer-dimer contact region, the dissociation rate is increased by approximately three orders of magnitude. In hemoglobin S where the amino acid substitution is not directly in the intersubunit contact region of interest, the dissociation rate is found to be approximately the same as that for hemoglobin A. Combination of the dissociation rate constants determined by haptoglobin binding with stopped-flow determinations of the rate constant for reassociation of dissociated dimers provides an estimate of the equilibrium constant, 0K2, for the deoxyhemoglobin dimer-tetramer equilibrium. This estimate is independent of any assumptions regarding other energetic quantities, and yields a value of 2.54 +/- 0.7 X 10(10)M-1 (heme) in 0.1 M Tris-HCl, 0.1 M NaCl, and 1 mM EDTA, pH 7.4, 21.5 degrees C. Thus the intersubunit contact energy is -14.0 +/- 0.2 kcal/mol of heme. The stabilization energy between deoxy and oxy tetramers is found to be approximately 6.4 kcal/mol, under these conditions.

Binding Sites↗
PubMed1975

Kinetic studies on coenzyme binding and coenzyme dissociation in tryptophanase immobilized on sepharose.

The binding rate of pyridoxal '5-phosphate (Pxa-P) to apotryptophanase and the dissociation rate of the coenzyme from holotryptophanase were able to be determined by following the enzyme activity in continuous flow reactions on a column of immobilized tryptophanase. When the enzyme activity was assayed continuously in the flow system in the absence of coenzyme added to the reaction mixture, immobilized holotryptophanase lost gradually its initial activity owing to dissociation of coenzyme. The coenzyme dissociation at a given concentration of substrate (tryptophan) followed first-order kineticsmin a low substrate concentration range below the Km value, a more decreased rate constant was obtained for the coenzyme dissociation. This indicates that the coenzyme is more dissociable from the apoenzyme-coenzyme-substrate complex (ECS complex) rather than from the apoenzyme-coenzymecomplex (holoenzyme). Immobilized tryptophanase freed of coenzyme restored rapidly its original activity, when the assay mixture containing a given concentration of substrate and Pxa-P was passed through the immobilized enzyme column. The coenzyme binding at a given coenzyme concentration followed first-order kinetics, but the rate was not first order in regard to the coenzyme concentration. A plot of the reciprocal of the first-order rate constant obtained vs. the reciprocal of the coenzyme binding occurs in a two-step fashion; the first step is rapid and the second step is rate determining. Both the dissociation constant for the first step and the rate constant for the second step were shown to be independent of the substrate concentration. This means that Schiff base formation between Pxa-P and tryptophan in the assay mixture has no effect on the binding of Pxa-P to apoenzyme. The coenzyme dissociation constant at a given substrate concentration was calculated from both the rate constant of the coenzyme binding and the rate constant of the coenzyme dissociation. The values obtained by this method at different substrate concentrations were almost identical with those measured at the corresponding substrate concentrations directly by an ordinary method.

Apoenzymes↗
PubMed1975

The effects of salts on the subunit structure and dissociation of Lumbricus terrestris hemoglobin.

The effects of the neutral salts of the Hofmeister series, NaCl, NaClO4, MgCl2, NaI, and also guanidine hydrochloride (Gdn-HCl)on the subunit organization and the state of association of Lumbricus terrestris hemoglobin were examined by light scattering molecular weight measurements. The subunit dissociation of the parent duodecameric structure of 3 x 10(6) molecular weight by various salts is similar in pattern to the sequential splitting of the associated protein to half-molecules of hexamers of 1.5 x 10(6) molecular weight, followed by further dissociation at higher reagent concentration to monomers of 250000 molecular weight. Duodecamer to hexamer dissociation is observed in 0.4 M MgCl2, 1-2 M NaCl, and 1 M Gdn-HCl, while hexamer to monomer dissociation is seen in the presence of 1 M MgCl2. All three species of duodecamers, hexamers, and monomers seem to be present in 1 M NaClO4. Further splitting of the monomers of A subunits to smaller B fragments of one-third to one-quarter molecular weight is observed in 1 M NaI solutions. Optical rotation in the peptide region and absorption measurements in the Soret region indicate the salt dissociation of Lumbricus terrestris hemoglobin is not accompanied by major changes in the folding of the subunits, except in the case of the strong protein denaturant, Gdn-HCl. Relative to the dissociation effects of the urea series of compounds reported in the preceding paper (Herskovits and Harrington, 1975), the neutral salts appear to be much more effective dissociating agents for L. terrestris hemoglobin. This suggests that polar and ionic interactions are relatively more important for the maintenance of the protein than hydrophobic interactions. This conclusion is also supported by calculations of the possible effects of binding of NaClO4, based on the Setschenow constants of the literature describing the interaction of salts with the peptide and hydrophobic alkyl group of the average amino acid found in proteins, on the standard free energy of dissociation of the duodecamer to hexamer.

Animals↗
PubMed1975

Kinetic light scattering studies on the dissociation of hemoglobin from Lumbricus terrestris.

The kinetics of the pH-induced dissociation of the 3 X 10(6) mol wt hemoglobin from Lumbricus terrestris (the earthworm) have been studied in a light-scattering stopped-flow apparatus. The ligand dependent dissociation data were fit well by a simple sequential model. The data for CO and oxyhemoglobin are consistent with Hb12 leads to 2Hb6 leads to 12Hb. Methemoglobin at pH 7 appears to be hexameric and the dissociation is consistent with the model: Hb6 leads to 6Hb. In a sequential decay scheme for which light-scattering changes are monitored, the relative amounts of rapid and slow phase are determined by the rate constants as well as the molecular weights of intermediate species. Assignment of the hexameric intermediate is supported by an investigation of the sensitivity of the theoretical kinetic curves to the molecular weights of the intermediates. This assignment is further supported by the following: (1) the same model will fit the data for oxy- and CO-hemoglobin at all three temperatures (a 24-29-fold variation in rate constants), (2) evidence from electron microscopy shows hexameric forms, and (3) methemoglobin is apparently stable as a hexamer at pH 7. When CO replaces O2 as the ligand, the dissociation rate increases by a factor of four. The met is about 20 times faster than the initial oxyhemoglobin dissociation rate, but perhaps more relevant for comparing dissociation of the hexamer, the met rate was respectively 100 times and 500 times faster than that for the assumed hexameric forms of CO- and oxy-hemoglobin. The activation energies for the dodecamer to hexamer dissociation and for the dissociation of the hexamer to smaller forms were about 30 kcal/mol for oxy-, CO-, and methemoglobin.

Carbon Monoxide↗
PubMed2002

Conformational heterogeneity is revealed in the dissociation of the oligomeric chaperonin GroEL by high hydrostatic pressure.

We investigated the dissociation of tetradecameric GroEL by high hydrostatic pressure in the range of 1-2.5 kbar. Kinetics of the dissociation of GroEL in the absence and presence of Mg(2+) and/or KCl were monitored using light scattering. All of the kinetics were biphasic in nature. At any given pressure, only monomers and 14mers were produced, and below 2.5 kbar, the 14mers only partially dissociated to monomers, which did not significantly reassemble on depressurization. Under identical reaction conditions, the observed dissociation rates decreased by only 2-fold when the concentration of GroEL was increased by 20-fold. At 2.5 kbar the observed rates decreased exponentially with the increase in [KCl] and reached a minimum at approximately 75mM. Similarly, the rates decreased with the increase in [Mg(2+)] and reached a minimum at approximately 3 mM Mg(2+). In the presence of saturating amounts of Mg(2+) (10 mM) and KCl (100 mM), the rates were much faster than with 10 mM Mg(2+) alone. The results could be rationalized in terms of the presence of GroEL heterogeneity, which could not be assessed easily by common techniques such as sedimentation velocity, HPLC, gel electrophoresis, and dissociation by chaotropes. This heterogeneity is evidence of subpopulations of GroEL that dissociate at different pressures. At low pressures, the oligomer without added Mg(2+) only partially dissociates to monomers, leading to an apparent plateau in the kinetics, whereas in the presence of Mg(2+) the species are converted to a tighter Mg(2+)-bound species, leading to a much slower dissociation process. The presence of KCl in the sample also leads to similar heterogeneity.

Chaperonin 60↗
PubMed1997

Pressure-induced dissociation of yeast glyceraldehyde-3-phosphate dehydrogenase: heterogeneous kinetics and perturbations of subunit structure.

In studies of pressure-induced subunit dissociation of oligomeric proteins, the thermodynamic dissociation constant and the dissociation volume change are derived by assuming that high pressure itself does not significantly perturb the structure of both oligomer and isolated subunit. In this report, the intrinsic phosphorescence emission of Trp reveals that high-pressure dissociation of tetrameric yeast glyceraldehyde-3-phosphate dehydrogenase results in a dramatic shortening of the phosphorescence lifetime, from 300 to less than 2 ms, that is consistent with a profound loosening of the polypeptide structure about the phosphorescence probe. On pressure release, subunit reassociation occurs readily whereas recovery of the native phosphorescence properties is a very slow, thermally activated, process which goes hand in hand with the recovery of the catalytic activity. Further, the comparison between the kinetic traces that describe the degree of dissociation and the change in phosphorescence lifetime, at various applied pressures, has established the following: (1) that high pressure plays a direct role on the structural rearrangement, the extent of which increases with pressure; (2) that the conformational change in the monomer is concomitant with, or follows closely after, the break up of the tetramer, in any case long before an apparent tetramer-monomer equilibrium is established; (3) that native tetramers are highly heterogeneous with regard to their rate of dissociation. The influence of temperature, of protein concentration, of binding of NAD+, and of the addition of 2 M urea on the dissociation/phosphorescence kinetic profiles was also examined. The complications arising from these conformational changes for the derivation of the dissociation free energy change as well as their relevance for understanding the lack of concentration dependence of the degree of dissociation are discussed.

Adenosine Triphosphate↗
PubMed1998

Ligand binding to thrombin exosite II induces dissociation of the thrombin-heparin cofactor II(L444R) complex.

Heparin cofactor II (HCII) inhibits thrombin rapidly in the presence of heparin or dermatan sulfate. The product of the inhibition reaction is a kinetically stable, 1:1 complex between the two proteins. We recently observed that heparin induces dissociation of complexes containing thrombin and the reactive site mutant HCII(L444R) to yield active thrombin and cleaved inhibitor (Han, J. -H., Van Deerlin, V. M. D., and Tollefsen, D. M. (1997) J. Biol. Chem. 272, 8243-8249). In the current study, we have investigated the mechanism by which heparin induces dissociation of the thrombin-HCII(L444R) complex. Heparin oligosaccharides >/=6 sugars in length induce dissociation, which suggests that dissociation does not depend on binding of a heparin molecule simultaneously to both proteins in the complex. Binding of heparin to HCII(L444R) in the complex also does not appear to be required, since the heparin dose response is unaltered for complexes containing the double mutant HCII(L444R/K173Q), which has decreased affinity for heparin. By contrast, binding of heparin to thrombin appears to be necessary and sufficient to induce dissociation. First, heparin fails to induce dissociation of complexes that contain thrombin(K236E), a variant with decreased heparin affinity. Second, a monoclonal IgG that interacts with the heparin-binding site of thrombin mimicks heparin in its ability to induce dissociation of the thrombin-HCII(L444R) complex. Finally, the complex of HCII(L444R) with thrombin(desPPW), which binds normally to heparin but lacks Pro60BPro60CTrp60D in an insertion loop ("60-loop") between the heparin-binding site and the catalytic site, does not dissociate in the presence of heparin. These results suggest that binding of heparin to thrombin induces an allosteric effect causing destabilization of the thrombin-HCII(L444R) complex and that the allosteric effect may be mediated by the 60-loop.

Arginine↗
PubMed1999

Structural characterization of lactate dehydrogenase dissociation under high pressure studied by synchrotron high-pressure small-angle X-ray scattering.

The effect of high pressure on lactate dehydrogenase (LDH) was studied using small-angle X-ray scattering (SAXS). The SAXS results are interpreted in terms of the dissociation and association of LDH within a compression and decompression cycle and its temperature dependence. LDH consists of four identical subunits. At 120 MPa and 25 degrees C, 50% of the LDH dissociates into subunits, while at 10 degrees C, this occurs at 78 MPa. The hysteresis in the dissociation and association under pressure was confirmed in terms of the radius of gyration and was seen to be more conspicuous at low temperature. Forward scattering, I(0)/C, which is proportional to molecular weight, showed that LDH dissociated into dimer (not monomer) subunits under pressure. The application of high pressure to dissociated dimers induced irreversible aggregation. This result is in sharp contrast with the result of fluorescence spectroscopy suggesting a dissociated monomer [King, L., and Weber, G. (1986) Biochemistry 25, 3637-3640]. As for structural change after reassociation, there was little structural difference between native and drifted LDH. The difference was smaller than the structure change by ligand binding. At 200 MPa, the presence of five scattering peaks in the medium-angle region indicates that the dissociated dimer does not have a molten globule-like structure but a core structure. We propose a model of the dissociated dimer, based on the SAXS profile, in which the volume is reduced without disrupting the core structure.

Animals↗
PubMed2005

Enhancement of O2 dissociation on Au111 by adsorbed oxygen: implications for oxidation catalysis.

We show that the dissociation probability of O2 on the reconstructed, Au111-herringbone surface is dramatically increased by the presence of some atomic oxygen on the surface. Specifically, at 400 K the dissociation probability of O2 on oxygen precovered Au111 is on the order of 10(-3), whereas there is no measurable dissociation on clean Au111, establishing an upper bound for the dissociation probability of 10(-6). Atomic oxygen was deposited on the clean reconstructed Au111-herringbone surface using electron bombardment of condensed NO2 at 100 K. The dissociation probability for dioxygen was measured by exposing the surface to 18O2. Temperature programmed desorption (TPD) was used to quantify the amount of oxygen dissociation and to study the stability of the oxygen in all cases. Oxygen desorbs as O2 in a peak centered at 550 K with pseudo-first-order kinetics; i.e., the desorption peak does not shift with coverage. Our interpretation is that the coverage dependence of the activation energy for dissociation (deltaE(dis)) and/or preexponential factor (nu(d)) may be responsible for the unusual desorption kinetics, implying a possible energy barrier for O2 dissociation on Au111. These results are discussed in the context of Au oxidation chemistry and the relationship to supported Au nanoparticles.

Adsorption↗
PubMed2005

A study of the unimolecular dissociation of the 2-buten-2-yl radical via the 193 nm photodissociation of 2-chloro-2-butene.

This work investigates the unimolecular dissociation of the 2-buten-2-yl radical. This radical has three potentially competing reaction pathways: C-C fission to form CH3 + propyne, C-H fission to form H + 1,2-butadiene, and C-H fission to produce H + 2-butyne. The experiments were designed to probe the branching to the three unimolecular dissociation pathways of the radical and to test theoretical predictions of the relevant dissociation barriers. Our crossed laser-molecular beam studies show that 193 nm photolysis of 2-chloro-2-butene produces 2-buten-2-yl in the initial photolytic step. A minor C-Cl bond fission channel forms electronically excited 2-buten-2-yl radicals and the dominant C-Cl bond fission channel produces ground-state 2-buten-2-yl radicals with a range of internal energies that spans the barriers to dissociation of the radical. Detection of the stable 2-buten-2-yl radicals allows a determination of the translational, and therefore internal, energy that marks the onset of dissociation of the radical. The experimental determination of the lowest-energy dissociation barrier gave 31 +/- 2 kcal/mol, in agreement with the 32.8 +/- 2 kcal/mol barrier to C-C fission at the G3//B3LYP level of theory. Our experiments detected products of all three dissociation channels of unstable 2-buten-2-yl as well as a competing HCl elimination channel in the photolysis of 2-chloro-2-butene. The results allow us to benchmark electronic structure calculations on the unimolecular dissociation reactions of the 2-buten-2-yl radical as well as the CH3 + propyne and H + 1,2-butadiene bimolecular reactions. They also allow us to critique prior experimental work on the H + 1,2-butadiene reaction.

Journal Article↗
PubMed2005

F-loss and H-loss dissociations in low-lying electronic states of the CH3F+ ion studied using multiconfiguration second-order perturbation theory.

Complete active space self-consistent field (CASSCF) and multiconfiguration second-order perturbation theory (CASPT2) calculations with an atomic natural orbital basis were performed for the 1(2)A'', 1(2)A', 2(2)A', 2(2)A'', and 3(2)A' (X2E, A2A1, and B2E) states of the CH3F+ ion. The 1(2)A'' state is predicted to be the ground state, and the C(s)-state energy levels are different from those of the CH3Cl+ ion. The 2(2)A' (A2A1) state is predicted to be repulsive, and the calculated adiabatic excitation energies for 2(2)A'' and 3(2)A' are very close to the experimental value for the B state. The CASPT2//CASSCF potential energy curves (PECs) were calculated for F-loss dissociation from the five C(s) states and H-loss dissociation from the 1(2)A'', 1(2)A', and 2(2)A'' states. The electronic states of the CH3+ and CH2F+ ions as the dissociation products were carefully determined by checking the energies and geometries of the asymptote products, and appearance potentials for the two ions in different states are predicted. The F-loss PEC calculations for CH3F+ indicate that F-loss dissociation occurs from the 1(2)A'', 1(2)A', and 2(2)A' states [all correlating with CH3+(X1A1')], which supports the experimental observations of direct dissociation from the X and A states, and that direct F-loss dissociation can occur from the two Jahn-Teller component states of B2E, 2(2)A'' and 3(2)A' [correlating with CH3+(1(3)A'') and CH3+(1(3)A'), respectively]. Some aspects of the 3(2)A' Cl-loss PEC of the CH3Cl+ ion are inferred on the basis of the calculation results for CH3F+. The H-loss PEC calculations for CH3F+ indicate that H-loss dissociation occurs from the 1(2)A'', 1(2)A', and 2(2)A'' states [correlating with CH2F+(1(3)A''), CH2F+(X1A1), and CH2F+(1(1)A''), respectively], which supports the observations of direct dissociation from the X and B states. As the 2(2)A' H-loss PEC of CH3Cl+, the 2(2)A' H-loss PEC of CH3F+ does not lead to H + CH2X+, but the PECs of the two ions represent different types of reactions.

Journal Article↗
PubMed2006

Hydration and dissociation of hydrogen fluoric acid (HF).

The hydration and dissociation phenomena of HF(H(2)O)(n)() (n < or = 10) clusters have been studied by using both the density functional theory with the 6-311++G[sp] basis set and the Møller-Plesset second-order perturbation theory with the aug-cc-pVDZ+(2s2p/2s) basis set. The structures for n > or = 8 are first reported here. The dissociated form of the hydrogen-fluoric acid in HF(H(2)O)(n) clusters is found to be less stable at 0 K than the undissociated form until n = 10. HF may not be dissociated at 0 K solely by water molecules because the HF H bond is stronger than the OH H bond, against the expectation that the dissociated HF(H(2)O)(n) would be more stable than the undissociated one in the presence of a number of water molecules. The dissociation would be possible for only a fraction of a number of hydrated HF clusters by the Boltzmann distribution at finite temperatures. This is in sharp contrast to other hydrogen halide acids (HCl, HBr, HI) showing the dissociation phenomena at 0 K for n > or = 4. The IR spectra of dissociated and undissociated structures of HF(H(2)O)(n) are compared. The structures and binding energies of HF(H(2)O)(n) are found to be similar to those of (H(2)O)(n+1). It is interesting that HF(H(2)O)(n=5,6,10) are slightly less stable compared with other sizes of clusters, just like the fact that (H(2)O)(n=6,7,11) are slightly less stable. The present study would be useful for the experimental/spectroscopic investigation of not only the dissociation phenomena of HF but also the similarity of the HF-water clusters to the water clusters.

Journal Article↗