Evidence map›Paper›PMID 34280872›Full record

ReviewCurrent opinion in structural biology2022

Advances in optimizing enzyme electrostatic preorganization.

Matthew R Hennefarth, Anastassia N Alexandrova

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed.

  1. Metabolic Structure: A Paradigm Revisited in Light of the Fundamental Parameters of Living Systems.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. What Can be Learned From the Electrostatic Environments Within Nitrogenase Enzymes?Chemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  7. Preorganized Electric Fields in Voltage-Gated Sodium Channels.Chembiochem : a European journal of chemical biology · 2025
    Article
  8. Spatially Regulated Electrical Forces for Biological Catalysis.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Protein Dynamics and Enzymatic Catalysis.The journal of physical chemistry. B · 2023
    Review
  14. Article
  15. Article
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Matthew R HennefarthDepartment of Chemistry and Biochemistry, University of California, Los Angeles, 607 Charles E. Young Drive East, Los Angeles, CA 90095-1569, USA.
Anastassia N AlexandrovaDepartment of Chemistry and Biochemistry, University of California, Los Angeles, 607 Charles E. Young Drive East, Los Angeles, CA 90095-1569, USA; California NanoSystems Institute, University of California, Los Angeles, 570 Westwood Plaza, Los Angeles, CA 90095-1569, USA. Electronic address: ana@chem.ucla.edu.

Funding

Redox enzymes - tuning and designR01GM134047 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ALEXANDROVA, ANASTASSIA N, YANG, JENNY · 2019 to 2022
$1.3M
NIGMS NIH HHS R01 GM134047
6 · The paper itself

Abstract

Utilizing electric fields to catalyze chemical reactions is not a new idea, but in enzymology it undergoes a renaissance, inspired by Warhsel's concept of electrostatic preorganization. According to this concept, the source of the immense catalytic efficiency of enzymes is the intramolecular electric field that permanently favors the reaction transition state over the reactants. Within enzyme design, computational efforts have fallen short in designing enzymes with natural-like efficacy. The outcome could improve if long-range electrostatics (often omitted in current protocols) would be optimized. Here, we highlight the major developments in methods for analyzing and designing electric fields generated by the protein scaffolds, in order to both better understand how natural enzymes function, and aid artificial enzyme design.

Indexed as

EnzymesCatalysisStatic ElectricityEnzymesElectric fieldsElectrostatic preorganizationEnzymatic catalysisEnzyme designTheory

Identifiers

PMID34280872
PMCPMC8761209

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.