The DOI matches its Crossref record.
A Low-Barrier Hydrogen Bond in the Catalytic Triad of Serine Proteases
Abstract
Spectroscopic properties of chymotrypsin and model compounds indicate that a low-barrier hydrogen bond participates in the mechanism of serine protease action. A low-barrier hydrogen bond between Nδ1 of His 57 and the β-carboxyl group of Asp 102 in chymotrypsin can facilitate the formation of the tetrahedral adduct, and the nuclear magnetic resonance properties of this proton indicate that it is a low-barrier hydrogen bond. These conclusions are supported by the chemical shift of this proton, the deuterium isotope effect on the chemical shift, and the properties of hydrogen-bonded model compounds in organic solvents, including the hydrogen bond in cis -urocanic acid, in which the imidazole ring is internally hydrogen-bonded to the carboxyl group.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Proton Transfer 200 Years after von Grotthuss: Insights from Ab Initio Simulations
Marx, D. (2006) · ChemPhysChem · doi:10.1002/cphc.200600128 · Cited by 920
Aconitase as iron–sulfur protein, enzyme, and iron-regulatory protein
Beinert, H., Kennedy, M. C., & Stout, C. D. (1996) · Chemical Reviews · doi:10.1021/cr950040z · Cited by 606
Some influences of fluorine in bioorganic chemistry
O’Hagan, D., & Rzepa, H. S. (1997) · Chemical Communications · doi:10.1039/a604140j · Cited by 460
Serine peptidases: Classification, structure and function
Page, M. J., & Di Cera, E. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7565-9 · Cited by 438
MECHANISTIC ASPECTS OF ENZYMATIC CATALYSIS: Lessons from Comparison of RNA and Protein Enzymes
Narlikar, G. J., & Herschlag, D. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.19 · Cited by 262
Metadata
- Authors
- Frey, P. A., Whitt, S. A., & Tobin, J. B.
- Venue
- Science
- Published
- 1994-06-24
- Volume
- 264
- Issue
- 5167
- Pages
- 1927-1930
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1966964730
- Cited by
- 726
- References
- 0
- FWCI
- 21.87
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: A Low-Barrier Hydrogen Bond in the Catalytic Triad of Serine Proteases. https://app.cochat.ai/papers/10.1126/science.7661899
- The paper
- Frey, P. A., Whitt, S. A., & Tobin, J. B. (1994). A Low-Barrier Hydrogen Bond in the Catalytic Triad of Serine Proteases. Science. https://doi.org/10.1126/science.7661899
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
