Evidence map›Paper›PMID 23746260›Full record

ReviewAnnual review of biochemistry2013

Hydrogen tunneling links protein dynamics to enzyme catalysis.

Judith P Klinman, Amnon Kohen

Abstract readReview
In one paragraph

Review in Annual review of biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 papers.

0numbers the graph read from it
0cells of the map it votes in
175citing 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

175 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Quantum biology: From mechanisms to medicine.Clinical and translational medicine · 2026
    Review
  11. Review
  12. What is quantum biology?Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  13. Article
  14. Enzyme Catalytic Parameters and Evolution Across the Dissipation Plane.International journal of molecular sciences · 2026
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Quantum Effects in Evolution: Terrestrial Fine-Tuning of Magnetic Parameters.Computational and structural biotechnology journal · 2026
    Article
  20. Review

115 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.

Judith P KlinmanDepartment of Chemistry, California Institute for Quantitative Sciences, University of California, Berkeley, California 94720, USA. klinman@berkeley.edu
Amnon Kohen

Funding

Toward a Comprehensive Model for Enzyme CatalysisR01GM025765 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH P · 1985 to 2015
$7.1M
Tunneling and dynamic studies with DHFRR01GM065368 · NIGMS · UNIVERSITY OF IOWA · PI CHEATUM, CHRISTOPHER M · 2002 to 2017
$3.5M
DOPAMINE MONOOXYGENASE--MOLECULAR MECHANISMSR37GM025765 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH POLLOCK · 1990 to 1999
–
NIGMS NIH HHS GM025765NIGMS NIH HHS GM65368NIGMS NIH HHS R01 GM025765NIGMS NIH HHS R01 GM065368NIGMS NIH HHS R37 GM025765
6 · The paper itself

Abstract

The relationship between protein dynamics and function is a subject of considerable contemporary interest. Although protein motions are frequently observed during ligand binding and release steps, the contribution of protein motions to the catalysis of bond making/breaking processes is more difficult to probe and verify. Here, we show how the quantum mechanical hydrogen tunneling associated with enzymatic C-H bond cleavage provides a unique window into the necessity of protein dynamics for achieving optimal catalysis. Experimental findings support a hierarchy of thermodynamically equilibrated motions that control the H-donor and -acceptor distance and active-site electrostatics, creating an ensemble of conformations suitable for H-tunneling. A possible extension of this view to methyl transfer and other catalyzed reactions is also presented. The impact of understanding these dynamics on the conceptual framework for enzyme activity, inhibitor/drug design, and biomimetic catalyst design is likely to be substantial.

Indexed as

ThermodynamicsCatalysisEnzymesHydrogenKineticsModels, MolecularProtein ConformationProteinsEnzymesHydrogenProteins

Identifiers

PMID23746260
PMCPMC4066974

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.