Evidence map›Paper›PMID 28375745›Full record

ReviewAnnual review of biochemistry2017

Electric Fields and Enzyme Catalysis.

Stephen D Fried, Steven G Boxer

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 171 papers.

0numbers the graph read from it
0cells of the map it votes in
171citing papers in PubMed
14.4field-weighted citation impact, top 1% of its field
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

171 citing papers in PubMed, 445 citations in OpenAlex.

  1. Article
  2. Article
  3. Predicting Activation Barriers With Ring and Bond Critical Points in the Kemp Elimination Reaction.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. A Nonenzymatic Analogue of the Biosynthesis of Pyridoxal Vitamers.Journal of the American Chemical Society · 2026
    Article
  12. Photoisomerization detected in a fully wavelength-tunable rhodopsin mimic system.Acta crystallographica. Section D, Structural biology · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. Quinones operate as proton-collecting antennas in energy-transducing membranes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  17. Article
  18. The Discovery ofACS catalysis · 2026
    Article
  19. Article
  20. Article

111 more citing papers are in PubMed but not listed here.

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 at 2 institutions in 2 countries.

Stephen D FriedProteins and Nucleic Acid Chemistry Division, Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom; email: sf537@cam.ac.uk.
Steven G BoxerDepartment of Chemistry, Stanford University, Stanford, California 94305; email: sboxer@stanford.edu.
Medical Research Council · GBStanford University · US

Funding

Biophysical Studies of Macromolecules and Molecular AssembliesR35GM118044 · NIGMS · STANFORD UNIVERSITY · PI STEVEN G. BOXER · 2016 to 2026
$7.2M
NMR &CIDNP STUDIES OF MB MUTANTS &OLIGONUCLEOTIDE LOOPR01GM027738 · NIGMS · STANFORD UNIVERSITY · PI BOXER, STEVEN G. · 1985 to 2016
$4.3M
Membrane Fusion, Organization, and Dynamics Using Supported BilayersR01GM069630 · NIGMS · STANFORD UNIVERSITY · PI BOXER, STEVEN G. · 2004 to 2015
$3.8M
NIGMS NIH HHS R01 GM027738NIGMS NIH HHS R01 GM069630NIGMS NIH HHS R35 GM118044
6 · The paper itself

Abstract

What happens inside an enzyme's active site to allow slow and difficult chemical reactions to occur so rapidly? This question has occupied biochemists' attention for a long time. Computer models of increasing sophistication have predicted an important role for electrostatic interactions in enzymatic reactions, yet this hypothesis has proved vexingly difficult to test experimentally. Recent experiments utilizing the vibrational Stark effect make it possible to measure the electric field a substrate molecule experiences when bound inside its enzyme's active site. These experiments have provided compelling evidence supporting a major electrostatic contribution to enzymatic catalysis. Here, we review these results and develop a simple model for electrostatic catalysis that enables us to incorporate disparate concepts introduced by many investigators to describe how enzymes work into a more unified framework stressing the importance of electric fields at the active site.

Indexed as

Bacterial ProteinsBiocatalysisCatalytic DomainGene ExpressionHydrolasesKetosteroidsKineticsModels, ChemicalMolecular Dynamics SimulationMutationPseudomonasSpectrophotometry, InfraredStatic ElectricitySteroid IsomerasesThermodynamics4-chlorobenzoyl coenzyme A dehalogenaseBacterial ProteinsHydrolasesKetosteroidsSteroid Isomeraseselectric fieldsenzyme electrostaticsinfrared spectroscopypreorganizationprotein biophysicsvibrational Stark effect

Identifiers

PMID28375745
PMCPMC5600505
OpenAlexW2468618868

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.