scholarly journals A Preorganized Electric Field Leads to Minimal Geometrical Reorientation in the Catalytic Reaction of Ketosteroid Isomerase

2020 ◽  
Vol 142 (22) ◽  
pp. 9993-9998 ◽  
Author(s):  
Yufan Wu ◽  
Stephen D. Fried ◽  
Steven G. Boxer
Keyword(s):  
Electric Field ◽  
Catalytic Reaction ◽  
Ketosteroid Isomerase

scholarly journals A Preorganized Electric Field Leads to Minimal Geometrical Reorientation in the Catalytic Reaction of Ketosteroid Isomerase

2020 ◽  
Author(s):  
Yufan Wu ◽  
Stephen Fried ◽  
Steven Boxer
Keyword(s):  
Electric Field ◽  
Electric Fields ◽  
Ground State ◽  
Active Site ◽  
Electrostatic Interactions ◽  
Stark Effect ◽  
Structural Changes ◽  
Enzymatic Catalysis ◽  
Ketosteroid Isomerase ◽  
Computational Enzyme Design

<div><p>Electrostatic interactions play a pivotal role in enzymatic catalysis and are increasingly modeled explicitly in computational enzyme design; nevertheless, they are challenging to measure experimentally. Using vibrational Stark effect (VSE) spectroscopy, we have measured electric fields inside the active site of the enzyme ketosteroid isomerase (KSI). These studies have shown that these fields can be unusually large, but it has been unclear to what extent they specifically stabilize the transition state (TS) relative to a ground state (GS). In the following, we use crystallography and computational modeling to show that KSI’s intrinsic electric field is nearly perfectly oriented to stabilize the geometry of its reaction’s TS. Moreover, we find that this electric field adjusts the orientation of its substrate in the ground state so that the substrate needs to only undergo minimal structural changes upon activation to its TS. This work provides evidence that the active site electric field in KSI is preorganized to facilitate catalysis and provides a template for how electrostatic preorganization can be measured in enzymatic systems. <br></p></div>

scholarly journals Key factor for the anti-Arrhenius low-temperature heterogeneous catalysis induced by H+ migration: H+ coverage over support

2020 ◽  
Vol 56 (23) ◽  
pp. 3365-3368 ◽  
Author(s):  
Kota Murakami ◽  
Yuta Tanaka ◽  
Ryuya Sakai ◽  
Yudai Hisai ◽  
Sasuga Hayashi ◽  
...  
Keyword(s):  
Heterogeneous Catalysis ◽  
Low Temperature ◽  
Electric Field ◽  
Catalytic Reaction ◽  
Small Scale ◽  
Heterogeneous Catalytic Reaction ◽  
Heterogeneous Catalytic ◽  
On Demand ◽  
Novel Approach ◽  
Key Factor

Low-temperature heterogeneous catalytic reaction in an electric field is anticipated as a novel approach for on-demand and small-scale catalytic processes.

Three-Way Catalytic Reaction in an Electric Field for Exhaust Emission Control Application

2021 ◽  
Author(s):  
Toru Uenishi ◽  
Ayaka Shigemoto ◽  
Yuki Omori ◽  
Takuma Higo ◽  
Shuhei Ogo ◽  
...  
Keyword(s):  
Electric Field ◽  
Catalytic Reaction ◽  
Emission Control ◽  
Exhaust Emission ◽  
Control Application

Roles of electrostatic interaction in proteins

1996 ◽  
Vol 29 (1) ◽  
pp. 1-90 ◽  
Author(s):  
Haruki Nakamura
Keyword(s):  
Hydrogen Bonds ◽  
Electric Field ◽  
Electrostatic Interaction ◽  
Catalytic Reaction ◽  
Active Site ◽  
Electrostatic Interactions ◽  
Essential Role ◽  
Molecular Assembly ◽  
Dipole Interactions ◽  
Protein Molecules

Electrostatic effects play an essential role in specific molecular recognition and molecular assembly in many biologically important molecules. The specific electric field at the active site also regulates the catalytic reaction of a protein. Moreover, intramolecular or inter-subunit electrostatic interactions, such as saltbridges, hydrogen bonds, and charge-dipole interactions, are considered to work to stabilize protein molecules. Those electrostatic roles recently observed in proteins are reviewed with a description of the origins and principles of electrostatic forces, and analyses will be made using simple models to illuminate the physical basis.

scholarly journals Direct Look at the Electric Field in Ketosteroid Isomerase and Its Variants

ACS Catalysis ◽  
2020 ◽  
Vol 10 (17) ◽  
pp. 9915-9924 ◽  
Author(s):  
Matthew R. Hennefarth ◽  
Anastassia N. Alexandrova
Keyword(s):  
Electric Field ◽  
Ketosteroid Isomerase

scholarly journals Extreme electric fields power catalysis in the active site of ketosteroid isomerase

Science ◽  
2014 ◽  
Vol 346 (6216) ◽  
pp. 1510-1514 ◽  
Author(s):  
Stephen D. Fried ◽  
Sayan Bagchi ◽  
Steven G. Boxer
Keyword(s):  
Electric Field ◽  
Electric Fields ◽  
Active Site ◽  
Stark Effect ◽  
Catalytic Effect ◽  
Biomolecular Systems ◽  
Ketosteroid Isomerase ◽  
Rate Determining Step ◽  
Experimental Approaches ◽  
A Charge

Enzymes use protein architecture to impose specific electrostatic fields onto their bound substrates, but the magnitude and catalytic effect of these electric fields have proven difficult to quantify with standard experimental approaches. Using vibrational Stark effect spectroscopy, we found that the active site of the enzyme ketosteroid isomerase (KSI) exerts an extremely large electric field onto the C=O chemical bond that undergoes a charge rearrangement in KSI’s rate-determining step. Moreover, we found that the magnitude of the electric field exerted by the active site strongly correlates with the enzyme’s catalytic rate enhancement, enabling us to quantify the fraction of the catalytic effect that is electrostatic in origin. The measurements described here may help explain the role of electrostatics in many other enzymes and biomolecular systems.

scholarly journals Quantitative, directional measurement of electric field heterogeneity in the active site of ketosteroid isomerase

2012 ◽  
Vol 109 (6) ◽  
pp. E299-E308 ◽  
Author(s):  
A. T. Fafarman ◽  
P. A. Sigala ◽  
J. P. Schwans ◽  
T. D. Fenn ◽  
D. Herschlag ◽  
...  
Keyword(s):  
Electric Field ◽  
Active Site ◽  
Ketosteroid Isomerase ◽  
Field Heterogeneity

Catalytic Reaction Assisted by Plasma or Electric Field

2017 ◽  
Vol 17 (8) ◽  
pp. 726-738 ◽  
Author(s):  
Shuhei Ogo ◽  
Yasushi Sekine
Keyword(s):  
Electric Field ◽  
Catalytic Reaction

scholarly journals A Preorganized Electric Field Leads to Minimal Geometrical Reorientation in the Catalytic Reaction of Ketosteroid Isomerase

2020 ◽  
Author(s):  
Yufan Wu ◽  
Stephen Fried ◽  
Steven Boxer
Keyword(s):  
Electric Field ◽  
Electric Fields ◽  
Ground State ◽  
Active Site ◽  
Electrostatic Interactions ◽  
Stark Effect ◽  
Structural Changes ◽  
Enzymatic Catalysis ◽  
Ketosteroid Isomerase ◽  
Computational Enzyme Design

<div><p>Electrostatic interactions play a pivotal role in enzymatic catalysis and are increasingly modeled explicitly in computational enzyme design; nevertheless, they are challenging to measure experimentally. Using vibrational Stark effect (VSE) spectroscopy, we have measured electric fields inside the active site of the enzyme ketosteroid isomerase (KSI). These studies have shown that these fields can be unusually large, but it has been unclear to what extent they specifically stabilize the transition state (TS) relative to a ground state (GS). In the following, we use crystallography and computational modeling to show that KSI’s intrinsic electric field is nearly perfectly oriented to stabilize the geometry of its reaction’s TS. Moreover, we find that this electric field adjusts the orientation of its substrate in the ground state so that the substrate needs to only undergo minimal structural changes upon activation to its TS. This work provides evidence that the active site electric field in KSI is preorganized to facilitate catalysis and provides a template for how electrostatic preorganization can be measured in enzymatic systems. <br></p></div>

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