Evidence map›Paper›PMID 40012333›Full record

ArticleThe journal of physical chemistry letters2025

Determination of Thiol Protonation States by Sulfur X-ray Spectroscopy in Biological Systems.

Ryan D Ribson, Alec H Follmer, Jeffrey T Babicz, Victor Sosa Alfaro, Ryan G Hadt, Mark S Hunter, Mark A Wilson, Dimosthenis Sokaras, Roberto Alonso-Mori

Abstract read
In one paragraph

Article in The journal of physical chemistry letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

9 authors.

Ryan D RibsonLinac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.ORCID 0000-0002-3755-5777
Alec H FollmerDepartment of Chemistry, University of California, Davis, One Shields Avenue, Davis, California 95616, United States.ORCID 0000-0002-6244-6804
Jeffrey T BabiczLinac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.ORCID 0000-0002-1476-8390
Victor Sosa AlfaroLinac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.ORCID 0000-0001-8149-5137
Ryan G HadtDivision of Chemistry and Chemical Engineering, Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, California 91125, United States.ORCID 0000-0001-6026-1358
Mark S HunterLinac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.
Mark A WilsonDepartment of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, United States.ORCID 0000-0001-6317-900X
Dimosthenis SokarasSSRL, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.ORCID 0000-0001-8117-1933
Roberto Alonso-MoriLinac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States.ORCID 0000-0002-5357-0934

Funding

Structural Dynamics at LCLSP41GM139687 · NIGMS · STANFORD UNIVERSITY · PI HUNTER, MARK · 2021 to 2025
$7.5M
Understanding Geometric and Electronic Structure Contributions to Ground and Excited State Cu- and Ni-Catalyzed Cross-Coupling ReactionsR35GM142595 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI HADT, RYAN G · 2021 to 2025
$2.1M
Time-resolved structural studies of enzyme catalysis and regulationR35GM153337 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI Mark A. Wilson · 2024 to 2026
$1.0M
NIGMS NIH HHS P41 GM139687NIGMS NIH HHS R35 GM142595NIGMS NIH HHS R35 GM153337
6 · The paper itself

Abstract

Cysteine is one of the most functionally diverse of the proteinogenic amino acids, owing to its reactive thiol side chain that can undergo deprotonation to form a strongly nucleophilic thiolate. However, few techniques can directly interrogate sulfur charge and covalency in cysteine, particularly in proteins. X-ray spectroscopies provide an element specific probe of sulfur. We demonstrate the sensitivity of S Kβ and Kα X-ray emission spectroscopy (XES) to cysteine ionization and compare it to S K-edge X-ray absorption spectroscopy (XAS) in the physiologically relevant biomolecules l-cysteine and

Indexed as

AcetylcysteineCysteineProtonsSulfhydryl CompoundsSulfurSpectrometry, X-Ray EmissionX-Ray Absorption SpectroscopyAcetylcysteineCysteineProtonsSulfhydryl CompoundsSulfur

Identifiers

PMID40012333
PMCPMC11892467

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.