scholarly journals Chemical mapping exposes the importance of active site interactions in governing the temperature dependence of enzyme turnover

2021 ◽  
Author(s):  
Samuel D Winter ◽  
Hannah BL Jones ◽  
Dora Rasadean ◽  
Rory Crean ◽  
Michael J. Danson ◽  
...  
Keyword(s):  
Heat Capacity ◽  
Temperature Dependence ◽  
Protein Dynamics ◽  
Active Site ◽  
Glucose Dehydrogenase ◽  
Global Changes ◽  
Global Dynamics ◽  
Specific Substrate ◽  
Substrate Interactions ◽  
Enzyme Turnover

Uncovering the role of global protein dynamics in enzyme turnover is needed to fully understand enzyme catalysis. Recently, we have demonstrated that the heat capacity of catalysis can reveal links between the protein free energy landscape, global protein dynamics and enzyme turnover, suggesting that subtle changes molecular interactions at the active site can affect long range protein dynamics and link to enzyme temperature activity. Here we use a model promiscuous enzyme (Glucose dehydrogenase from Sulfolobus Solfataricus) to chemically map how individual substrate interactions affect the temperature dependence of enzyme activity and the network of motions throughout the protein. Utilizing a combination of kinetics, REES spectroscopy and computational simulation we explore the complex relationship between enzyme-substrate interactions and the global dynamics of the protein. We find that changes in the heat capacity of catalysis and protein dynamics can be mapped to specific substrate-enzyme interactions. Our study reveals how subtle changes in substrate binding affect global changes in motion and flexibility extending throughout the protein.

scholarly journals Chemical Mapping Exposes the Importance of Active Site Interactions in Governing the Temperature Dependence of Enzyme Turnover

ACS Catalysis ◽  
2021 ◽  
pp. 14854-14863
Author(s):  
Samuel D. Winter ◽  
Hannah B. L. Jones ◽  
Dora M. Răsădean ◽  
Rory M. Crean ◽  
Michael J. Danson ◽  
...  
Keyword(s):  
Temperature Dependence ◽  
Active Site ◽  
Chemical Mapping ◽  
Enzyme Turnover

ABOUT HEAT CAPACITY OF TITANIUM CARBIDE TiCx

2019 ◽  
pp. 56-66
Author(s):  
I. Khidirov ◽  
V. V. Getmanskiy ◽  
A. S. Parpiev ◽  
Sh. A. Makhmudov
Keyword(s):  
Heat Capacity ◽  
High Temperature ◽  
Titanium Carbide ◽  
Temperature Dependence ◽  
Carbon Concentration ◽  
Room Temperature ◽  
Thermodynamic Characteristics ◽  
Liquid Nitrogen Temperature ◽  
Analysis Data ◽  
Thermal Excitation

This work relates to the field of thermophysical parameters of refractory interstitial alloys. The isochoric heat capacity of cubic titanium carbide TiCx has been calculated within the Debye approximation in the carbon concentration  range x = 0.70–0.97 at room temperature (300 K) and at liquid nitrogen temperature (80 K) through the Debye temperature established on the basis of neutron diffraction analysis data. It has been found out that at room temperature with decrease of carbon concentration the heat capacity significantly increases from 29.40 J/mol·K to 34.20 J/mol·K, and at T = 80 K – from 3.08 J/mol·K to 8.20 J/mol·K. The work analyzes the literature data and gives the results of the evaluation of the high-temperature dependence of the heat capacity СV of the cubic titanium carbide TiC0.97 based on the data of neutron structural analysis. It has been proposed to amend in the Neumann–Kopp formula to describe the high-temperature dependence of the titanium carbide heat capacity. After the amendment, the Neumann–Kopp formula describes the results of well-known experiments on the high-temperature dependence of the heat capacity of the titanium carbide TiCx. The proposed formula takes into account the degree of thermal excitation (a quantized number) that increases in steps with increasing temperature.The results allow us to predict the thermodynamic characteristics of titanium carbide in the temperature range of 300–3000 K and can be useful for materials scientists.

On Temperature Dependence of Excess Gibbs Energy

1999 ◽  
Vol 64 (7) ◽  
pp. 1093-1099 ◽  
Author(s):  
Ivona Malijevská ◽  
Anatol Malijevský
Keyword(s):  
Heat Capacity ◽  
Gibbs Energy ◽  
Temperature Dependence ◽  
Excess Gibbs Energy ◽  
Excess Enthalpy ◽  
Excess Heat Capacity ◽  
Wilson Equation ◽  
Excess Heat ◽  
Energy Excess ◽  
Wilson And Nrtl Equations

Temperature dependence of GE is discussed for three widely used equations linear and nonlinear in parameters. It is shown that the Wilson equation predicts always positive excess heat capacity regardless of values of its parameters. Several temperature modifications of the Redlich-Kister, Wilson and NRTL equations are discussed with respect to the sign of the excess Gibbs energy, excess enthalpy and excess heat capacity.

Heat capacity of activation for the hydrolysis of methanesulfonyl chloride and benzenesulfonyl chloride in light and heavy water

1969 ◽  
Vol 47 (22) ◽  
pp. 4199-4206 ◽  
Author(s):  
R. E. Robertson ◽  
B. Rossall ◽  
S. E. Sugamori ◽  
L. Treindl
Keyword(s):  
Heat Capacity ◽  
Free Energy ◽  
Temperature Dependence ◽  
Heavy Water ◽  
Bond Formation ◽  
Sulfonyl Chlorides ◽  
Benzenesulfonyl Chloride ◽  
Methanesulfonyl Chloride ◽  
Hydrolysis Of ◽  
Parameter Temperature Dependence

Rates of solvolysis of methanesulfonyl chloride and benzenesulfonyl chloride have been determined in H2O and D2O. The free energy, enthalpy, entropy, and heat capacity of activation were calculated. The exceptional accuracy of the data permitted an estimation of dΔCp≠/dT from a four parameter temperature dependence of the kinetic rates.From these data we conclude that both sulfonyl chlorides hydrolyse by the same mechanism (Sn2) The change in R from CH3 to C6H5 in RSO2Cl did not alter ΔCp≠ but ΔS≠ (20°) was changed from −8.32 to −13.25 cal deg−1 mole−1, respectively. The significance of this difference is attributed to the probability of bond formation rather than to differences in solvent reorganization.

Temperature dependence of the heat capacity of some titanium alloys

1967 ◽  
Vol 9 (6) ◽  
pp. 452-453 ◽  
Author(s):  
V. D. Sukhanov ◽  
Yu. N. Tsiovkin
Keyword(s):  
Heat Capacity ◽  
Temperature Dependence ◽  
Titanium Alloys

scholarly journals Change in Heat Capacity for Enzyme Catalysis Determines Temperature Dependence of Enzyme Catalyzed Rates

2017 ◽  
Vol 12 (3) ◽  
pp. 868-868 ◽  
Author(s):  
Joanne K. Hobbs ◽  
Wanting Jiao ◽  
Ashley D. Easter ◽  
Emily J. Parker ◽  
Louis A. Schipper ◽  
...  
Keyword(s):  
Heat Capacity ◽  
Temperature Dependence ◽  
Enzyme Catalysis

scholarly journals Temperature dependence of the specific heat and thermodynamic functions AК1М2 alloy, doped strontium

2019 ◽  
Vol 21 (1) ◽  
pp. 35-42 ◽  
Author(s):  
I. N. Ganiev ◽  
S. E. Otajonov ◽  
N. F. Ibrohimov ◽  
M. Mahmudov
Keyword(s):  
Heat Capacity ◽  
Gibbs Energy ◽  
Specific Heat ◽  
Temperature Dependence ◽  
Specific Heat Capacity ◽  
Thermodynamic Functions ◽  
Inverse Relationship ◽  
Alloying Element ◽  
Enthalpy And Entropy ◽  
Increasing Temperature

In the heat «cooling» investigated the temperature dependence of the specific heat capacity and thermodynamic functions doped strontium alloy AK1М2 in the range 298,15—900 K. Mathematical models are obtained that describe the change in these properties of alloys in the temperature range 298.15—900 K, as well as on the concentration of the doping component. It was found that with increasing temperature, specific heat capacity, enthalpy and entropy alloys increase, and the concentration up to 0.5 wt.% of the alloying element decreases. Gibbs energy values have an inverse relationship, i.e., temperature — decreases the content of alloying component — is up to 0.5 wt.% growing.

scholarly journals Active site residues and mechanism of UDP-glucose dehydrogenase

2003 ◽  
Vol 271 (1) ◽  
pp. 14-22 ◽  
Author(s):  
Xue Ge ◽  
Lisa C. Penney ◽  
Ivo Van De Rijn ◽  
Martin E. Tanner
Keyword(s):  
Active Site ◽  
Glucose Dehydrogenase ◽  
Active Site Residues
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