• Journal of the Korean Chemical Society
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• v.65 no.6
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• pp.419-432
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• 2021

According to the transition state (TS) theory, Gaussian software and Yao and Lin (YL) method, the thermodynamics and kinetic data respectively were calculated, and anharmonic effect was considered for related reactions of NO₃. The methods of calculating and fitting kinetic and thermodynamics parameters were provided by least square method and related equations in this paper. Notably, the fitted E of Arrhenius equation was close to the calculated barrier of related reaction by QCISD(T) method. Therefore, the kinetic fitting result can well express the physical meaning of E in Arrhenius equation. Besides, the conversion process and the reaction mechanism of NO₃ were researched. For NO₃, it seemed that its instability results from its easy reaction with other substances rather than the decompose reaction of itself.

• BMB Reports
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• v.39 no.2
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• pp.167-170
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• 2006

Bovine adenosine deaminase undergoes a nondenaturational conformational change at $29^{\circ}C$ upon heating which is characterized by a large increase in heat capacity. We have determined the transition state thermodynamics of the conformational change using a novel application of differential scanning calorimetry (DSC) which employs very slow scan rates. DSC scans at the conventional, and arbitrary, scan rate of $1^{\circ}C/min$ show no evidence of the transition. Scan rates from 0.030 to $0.20^{\circ}C/min$ reveal the transition indicating it is under kinetic control. The transition temperature $T_t$ and the transition temperature interval ${\Delta}T$ increase with scan rate. A first order rate constant $k_1$ is calculated at each $T_t$ from $k_1\;=\;r_{scan}/{\Delta}T$, where $r_{scan}$ is the scan rate, and an Arrhenius plot is constructed. Standard transition state analysis reveals an activation free energy ${\Delta}G^{\neq}$ of 88.1 kJ/mole and suggests that the conformational change has an unfolding quality that appears to be on the direct path to the physiological-temperature conformer.

• BMB Reports
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• v.40 no.2
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• pp.205-211
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• 2007

The stability curve - a plot of the Gibbs free energy of unfolding versus temperature - is calculated for bovine erythrocyte carbonic anhydrase in 150 mM sodium phosphate (pH = 7.0) from a combination of reversible differential scanning calorimetry measurements and isothermal guanidine hydrochloride titrations. The enzyme possesses two stable folded conformers with the conformational transition occurring at ~30$^{\circ}C$. The methodology yields a stability curve for the complete unfolding of the enzyme below this temperature but only the partial unfolding, to the molten globule state, above it. The transition state thermodynamics for the low- to physiological-temperature conformational change are calculated from slow-scan-rate differential scanning calorimetry measurements where it is found that the free energy barrier for the conversion is 90 kJ/mole and the transition state possesses a substantial unfolding quality. The data therefore suggest that the x-ray structure may differ considerably from the physiological structure and that the two conformers are not readily interconverted.

• Textile Coloration and Finishing
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• v.10 no.3
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• pp.36-42
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• 1998

The dyeabilities of C.I. Reactive Blue 19(B19, MW ; 626), C.I. Reactive Blue 4(B4, MW ; 637) and C.I. Reactive Black 5(B5, MW : 991) were investigated. Initial dyeing rates were increased and the amount of dye on the fabric at equilibrium was decreased with temperature like other ordinary dyeing processes. Activation entropy$(\Delta{S}^*)$ was decreased because of loose bonding between dyestuffes and fiber molecules at transition state. It can be clarified that the entire reaction is exothermic and the number of molecular species at transition state becomes greater from decrease in activation enthalpy$(\Delta{H}^*)$ and the increase in activation free energy$(\Delta{G}^*)$ with temperature, respectively. The amount of B19 on the fabric at equilibrium was greater than that of B4, because B4 became unreactive towards textile substrates through hydrolysis. Due to the biggest size of the dye molecule, the reaction rate of B5 was the slowest but its difunctional group played an important role in achieving the greatest amount of dye on the fabric at equilibrium.

• Korean Journal of Materials Research
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• v.21 no.2
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• pp.73-77
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• 2011

Specific heat of a crystal is the sum of electronic specific heat, which is the specific heat of conduction electrons, and lattice specific heat, which is the specific heat of the lattice. Since properties such as crystal structure and Debye temperature do not change even in the superconducting state, the lattice specific heat may remain unchanged between the normal and the superconducting state. The difference of specific heat between the normal and superconducting state may be caused only by the electronic specific heat difference between the normal and superconducting states. Critical temperature, at which transition occurs, becomes lower than $T_{c0}$ under the influence of a magnetic field. It is well known that specific heat also changes abruptly at this critical temperature, but magnetic field dependence of jump of specific heat has not yet been developed theoretically. In this paper, specific heat jump of superconducting crystals at low temperature is derived as an explicit function of applied magnetic field H by using the thermodynamic relations of A. C. Rose-Innes and E. H. Rhoderick. The derived specific heat jump is compared with experimental data for superconducting crystals of $MgCNi_3$, $LiTi_2O_4$ and $Nd_{0.5}Ca_{0.5}MnO_3$. Our specific heat jump function well explains the jump up or down phenomena of superconducting crystals.

• BMB Reports
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• v.40 no.4
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• pp.453-458
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• 2007

Bacterial luciferase is a heterodimeric enzyme, which catalyzes the light emission reaction, utilizing reduced FMN (FMNH2), a long chain aliphatic aldehyde and $O_2$, to produce green-blue light. This enzyme can be readily classed as slow or fast decay based on their rate of luminescence decay in a single turnover. Mutation of Glu175 in $\alpha$ subunit to Gly converted slow decay Xenorhabdus Luminescence luciferase to fast decay one. The following studies revealed that changing the luciferase flexibility and lake of Glu-flavin interactions are responsible for the unusual kinetic properties of mutant enzyme. Optical and thermodynamics studies have caused a decrease in free energy and anisotropy of mutant enzyme. Moreover, the role of Glu175 in transition state of folding pathway by use of stopped-flow fluorescence technique has been studied which suggesting that Glu175 is not involved in transition state of folding and appears as surface residue of the nucleus or as a member of one of a few alternative folding nuclei. These results suggest that mutation of Glu175 to Gly extended the structure of Xenorhabdus Luminescence luciferase, locally.