Evidence map›Paper›PMID 29250456›Full record

ArticleACS catalysis2017

Enhanced Rigidification within a Double Mutant of Soybean Lipoxygenase Provides Experimental Support for Vibronically Nonadiabatic Proton-Coupled Electron Transfer Models.

Shenshen Hu, Alexander V Soudackov, Sharon Hammes-Schiffer, Judith P Klinman

Open access · bronzeAbstract read
In one paragraph

Article in ACS catalysis, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

26 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. A Foundational Shift in Models for Enzyme Function.Journal of the American Chemical Society · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Biochemistry · 2023
    Article
  11. Review
  12. Heavy-Atom Quantum Tunnelling in Spin Crossovers of Nitrenes.Angewandte Chemie (International ed. in English) · 2022
    Article
  13. Article
  14. Proton-Coupled Electron Transfer Guidelines, Fair and Square.Journal of the American Chemical Society · 2021
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Moving Through Barriers in Science and Life.Annual review of biochemistry · 2019
    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

4 authors at 2 institutions in 1 country.

Shenshen HuDepartment of Chemistry, Department of Molecular and Cell Biology, and California Institute for Quantitative Biosciences, University of California, Berkeley, California 94720, United States.
Alexander V SoudackovDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
Sharon Hammes-SchifferDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
Judith P KlinmanDepartment of Chemistry, Department of Molecular and Cell Biology, and California Institute for Quantitative Biosciences, University of California, Berkeley, California 94720, United States.
QB3 · USUniversity of Illinois Urbana-Champaign · US

Funding

Looking in New Directions for Origins and Cryptic Mechanisms of Enzyme CatalysisR35GM118117 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH P · 2016 to 2025
$7.5M
Simulation of Proton and Hydride Transfer in EnzymesR37GM056207 · NIGMS · YALE UNIVERSITY · PI HAMMES-SCHIFFER, SHARON · 2011 to 2020
$3.2M
SIMULATION OF PROTON AND HYDRIDE TRANSFER IN ENZYMESR01GM056207 · NIGMS · UNIVERSITY OF NOTRE DAME · PI HAMMES-SCHIFFER, SHARON · 1998 to 2010
$2.7M
NIGMS NIH HHS R01 GM056207NIGMS NIH HHS R35 GM118117NIGMS NIH HHS R37 GM056207
6 · The paper itself

Abstract

Soybean lipoxygenase (SLO) is a prototype for nonadiabatic hydrogen tunneling reactions and, as such, has served as the subject of numerous theoretical studies. In this work, we report a nearly temperature-independent kinetic isotope effect (KIE) with an average KIE value of 661 ± 27 for a double mutant (DM) of SLO at six temperatures. The data are well-reproduced within a vibronically nonadiabatic proton-coupled electron transfer model in which the active site has become rigidified compared to wild-type enzyme and single-site mutants. A combined temperature-pressure perturbation further shows that temperature-dependent global motions within DM-SLO are more resistant to perturbation by elevated pressure. These findings provide strong experimental support for the model of hydrogen tunneling in SLO, where optimization of both local protein and ligand motions and distal conformational rearrangements is a prerequisite for effective proton vibrational wave function overlap between the substrate and the active-site iron cofactor.

Identifiers

PMID29250456
PMCPMC5724529
OpenAlexW2606112812

What OpenQuestion holds

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Registered trials

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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.