Evidence map›Paper›PMID 40498961›Full record

ArticleJournal of the American Chemical Society2025

Description of the Electronic Structure of Oxyhemoglobin Using Fe L-Edge X-ray Absorption Spectroscopy.

Augustin Braun, Charles J Titus, Leland B Gee, Michael L Baker, Max D J Waters, James J Yan, Sang-Jun Lee, Dennis Nordlund, William B Doriese, Galen C O'Neil and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. 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

15 authors.

Augustin BraunDepartment of Chemistry, Stanford University, Stanford, California 94305, United States.ORCID 0000-0002-9487-5769
Charles J TitusStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, California 94025, United States.
Leland B GeeDepartment of Chemistry, Stanford University, Stanford, California 94305, United States.
Michael L BakerDepartment of Chemistry, Stanford University, Stanford, California 94305, United States.ORCID 0000-0002-8246-3177
Max D J WatersDepartment of Chemistry, Stanford University, Stanford, California 94305, United States.ORCID 0000-0002-3505-627X
James J YanDepartment of Chemistry, Stanford University, Stanford, California 94305, United States.ORCID 0000-0001-5516-3446
Sang-Jun LeeStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, California 94025, United States.ORCID 0000-0002-8199-3993
Dennis NordlundStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, California 94025, United States.
William B DorieseNational Institute of Standards and Technology, Boulder, Colorado 80305, United States.ORCID 0000-0003-1107-6441
Galen C O'NeilNational Institute of Standards and Technology, Boulder, Colorado 80305, United States.ORCID 0000-0003-3450-2263
Daniel R SchmidtNational Institute of Standards and Technology, Boulder, Colorado 80305, United States.
Daniel S SwetzNational Institute of Standards and Technology, Boulder, Colorado 80305, United States.
Joel N UllomNational Institute of Standards and Technology, Boulder, Colorado 80305, United States.
Kent D IrwinDepartment of Physics, Stanford University, Stanford, California 94305, United States.
Edward I SolomonDepartment of Chemistry, Stanford University, Stanford, California 94305, United States.ORCID 0000-0003-0291-3199

Funding

Spectroscopic Characterization of Oxygen Intermediates in Non-heme and Heme Iron EnzymesR35GM145202 · NIGMS · STANFORD UNIVERSITY · PI EDWARD I SOLOMON · 2022 to 2026
$2.0M
Electronic Structure of Heme Enzyme Intermediates from Resonant Inelastic X-ray Scattering and L-Edge X-ray Absorption SpectroscopyF32GM122194 · NIGMS · STANFORD UNIVERSITY · PI GEE, LELAND BRUCE · 2017 to 2020
$227k
NIGMS NIH HHS F32 GM122194NIGMS NIH HHS R35 GM145202
6 · The paper itself

Abstract

The electronic structure of oxyhemoglobin has been controversial since the discovery of the compound's diamagnetism in 1936. This study uses partial fluorescence yield Fe L-edge X-ray absorption spectroscopy (XAS) in the 3s→2p fluorescence on oxyhemoglobin solutions, measured using a transition-edge sensor detector, to obtain a quantitative experimental description of the electronic structure of the O

Identifiers

PMID40498961
PMCPMC12797434

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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.