Methods for Theoretical Treatment of Local Fields in Proteins and Enzymes
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F25%3A43932872" target="_blank" >RIV/60461373:22340/25:43932872 - isvavai.cz</a>
Result on the web
<a href="https://pubs.acs.org/doi/full/10.1021/acs.chemrev.4c00471" target="_blank" >https://pubs.acs.org/doi/full/10.1021/acs.chemrev.4c00471</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.chemrev.4c00471" target="_blank" >10.1021/acs.chemrev.4c00471</a>
Alternative languages
Result language
angličtina
Original language name
Methods for Theoretical Treatment of Local Fields in Proteins and Enzymes
Original language description
Electric fields generated by protein scaffolds are crucial in enzymatic catalysis. This review surveys theoretical approaches for detecting, analyzing, and comparing electric fields, electrostatic potentials, and their effects on the charge density within enzyme active sites. Pioneering methods like the empirical valence bond approach rely on evaluating ionic and covalent resonance forms influenced by the field. Strategies employing polarizable force fields also facilitate field detection. The vibrational Stark effect connects computational simulations to experimental Stark spectroscopy, enabling direct comparisons. We highlight how protein dynamics induce fluctuations in local fields, influencing enzyme activity. Recent techniques assess electric fields throughout the active site volume rather than only at specific bonds, and machine learning helps relate these global fields to reactivity. Quantum theory of atoms in molecules captures the entire electron density landscape, providing a chemically intuitive perspective on field-driven catalysis. Overall, these methodologies show protein-generated fields are highly dynamic and heterogeneous, and understanding both aspects is critical for elucidating enzyme mechanisms. This holistic view empowers rational enzyme engineering by tuning electric fields, promising new avenues in drug design, biocatalysis, and industrial applications. Future directions include incorporating electric fields as explicit design targets to enhance catalytic performance and biochemical functionalities.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10403 - Physical chemistry
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
CHEMICAL REVIEWS
ISSN
0009-2665
e-ISSN
1520-6890
Volume of the periodical
125
Issue of the periodical within the volume
7
Country of publishing house
US - UNITED STATES
Number of pages
42
Pages from-to
3772-3813
UT code for WoS article
001432707500001
EID of the result in the Scopus database
2-s2.0-105002491027