Evidence map›Paper›PMID 41717823›Full record

ArticleJournal of agricultural and food chemistry2026

Resonance Raman Spectroscopy and Density Functional Theory Reveal the Hemin Release Mechanism of Fish and Mammalian Hemoglobin.

Sean M Baker, Ryan L Hall, Thomas C Brunold, Mark P Richards

Abstract read
In one paragraph

Article in Journal of agricultural and food chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

4 authors.

Sean M BakerDepartment of Food Science, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID 0000-0001-6432-2277
Ryan L HallDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.
Thomas C BrunoldDepartment of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.ORCID 0000-0001-6516-598X
Mark P RichardsDepartment of Food Science, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Salmonids are an incredibly valuable agricultural commodity, with large market growth expected over the next 10 years. Salmonids have a high feed conversion ratio and are rich in vital nutrients; however, their post-mortem tissues are subject to deterioration due in part to their labile hemoglobin (Hb). In this work, we aimed to understand the driving force for the pro-oxidative nature of salmonid (trout IV) Hb. We utilized resonance Raman spectroscopy (rR), electronic absorption spectroscopy (EA), and density functional theory (DFT) calculations to probe the distal and proximal heme pocket architectures of trout IV and bovine Hb. Using fluoride as a H-bond-sensitive ligand, we found that at low pH, trout IV ferric Hb is more likely to have a protonated distal His. The enhanced distal His protonation and mobility play a crucial role in hemin dissociation, explaining the oxidative capacity of salmonid Hb, which dwarfs that of mammalian Hb.

Indexed as

Fish ProteinsHeminHemoglobinsAnimalsCattleDensity Functional TheoryHydrogen-Ion ConcentrationOxidation-ReductionSpectrum Analysis, RamanTroutFish ProteinsHeminHemoglobinsDFT computationshemin dissociationresonance Raman

Identifiers

PMID41717823
PMCPMC12964545

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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.