Evidence map›Paper›PMID 27162964›Full record

ArticleACS central science2015

Short Hydrogen Bonds and Proton Delocalization in Green Fluorescent Protein (GFP).

Luke M Oltrogge, Steven G Boxer

Abstract read
In one paragraph

Article in ACS central science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Low-barrier hydrogen bond powers long-range radical transfer in the metal-free ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
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  7. Free-Base Corrole Anion.The Journal of organic chemistry · 2023
    Article
  8. Article
  9. Review
  10. Review
  11. Article
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  13. Article
  14. Article
  15. Article
  16. On the Case of the Misplaced Hydrogens.Chembiochem : a European journal of chemical biology · 2021
    Review
  17. Article
  18. Low barrier hydrogen bonds in protein structure and function.Biochimica et biophysica acta. Proteins and proteomics · 2021
    Review
  19. Article
  20. 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.

Luke M OltroggeDepartment of Chemistry, Stanford University , Stanford, California 94305-5012, United States.
Steven G BoxerDepartment of Chemistry, Stanford University , Stanford, California 94305-5012, United States.

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
ELECTROSTATICS AND DYNAMICS IN MYOGLOBIN MUTANTSR37GM027738 · NIGMS · STANFORD UNIVERSITY · PI BOXER, STEVEN G. · 1994 to 2003
$1.2M
NIGMS NIH HHS R01 GM027738NIGMS NIH HHS R35 GM118044NIGMS NIH HHS R37 GM027738
6 · The paper itself

Abstract

Short hydrogen bonds and specifically low-barrier hydrogen bonds (LBHBs) have been the focus of much attention and controversy for their possible role in enzymatic catalysis. The green fluorescent protein (GFP) mutant S65T, H148D has been found to form a very short hydrogen bond between Asp148 and the chromophore resulting in significant spectral perturbations. Leveraging the unique autocatalytically formed chromophore and its sensitivity to this interaction we explore the consequences of proton affinity matching across this putative LBHB. Through the use of noncanonical amino acids introduced through nonsense suppression or global incorporation, we systematically modify the acidity of the GFP chromophore with halogen substituents. X-ray crystal structures indicated that the length of the interaction with Asp148 is unchanged at ∼2.45 Å while the absorbance spectra demonstrate an unprecedented degree of color tuning with increasing acidity. We utilized spectral isotope effects, isotope fractionation factors, and a simple 1D model of the hydrogen bond coordinate in order to gain insight into the potential energy surface and particularly the role that proton delocalization may play in this putative short hydrogen bond. The data and model suggest that even with the short donor-acceptor distance (∼2.45 Å) and near perfect affinity matching there is not a LBHB, that is, the barrier to proton transfer exceeds the H zero-point energy.

Identifiers

PMID27162964
PMCPMC4827562

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.