Evidence map›Paper›PMID 40665777›Full record

ReviewActa physiologica (Oxford, England)2025

Christian Bohr. Discoverer of Homotropic and Heterotopic Allostery: Periods Leading up to Bohr's Life, Work, and Beyond. Was Bohr a Vitalist and Right About a "Specific Activity"?

Niels Bindslev

Abstract readHistorical ArticleReview
In one paragraph

Review in Acta physiologica (Oxford, England), 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

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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. Review
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

1 author.

Niels BindslevEmeritus, BMI, Panum Institute, Copenhagen University, Copenhagen, Denmark.ORCID 0000-0002-6682-0947

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This essay recounts and revisits the scientific contributions of Christian Bohr, highlighting his pivotal role in discovering allostery about 120 years ago. Bohr's meticulous experimentation led to identifying two distinct forms of allostery: homotropic (single-ligand) and heterotropic (multi-ligand), the latter widely recognized as the Bohr Effect. His insights into oxygen binding to hemoglobin, as also modulated by carbon dioxide presence, laid the foundation for part of modern pharmacological advancements. Today, allosteric principles drive drug development, improving specificity and potentially minimizing adverse effects, with numerous allosteric modulators emerging in pharmaceutical pipelines. The treatise spans 13 chapters and an appendix with definitions on allosteric terms. It begins with Bohr's background, laboratory environment, and pivotal experiments in 1903 that demonstrated allosteric mechanisms. It traces Bohr's scientific journey-from medical training to his professorship in Copenhagen-and his collaborative research with Karl Hasselbalch and August Krogh. The work situates Bohr within the broader historical context, examining influence of earlier, 19th-century, and later physicochemical and physiological thoughts on his discoveries. Further chapters discuss dose-response relationships, including Hüfner's hyperbolic equation and Henri's enzyme kinetics, parallel to Bohr's findings. Bohr's S-shaped oxygen-hemoglobin binding curve, analyzed in 1904, marked a critical advancement in understanding homotropic allostery. Subsequent developments, such as Hill's equation and the Monod-Wyman-Changeux model, settled both types of allostery description. My study concludes with Bohr's abandonment in 1910 of his secretion theory and his legacy. Despite his early death in 1911, Bohr's contributions remain fundamental, warranting revitalized recognition for his discovery of allostery.

Indexed as

HemoglobinsOxygenAllosteric RegulationHistory, 19th CenturyHistory, 20th CenturyHumansHemoglobinsOxygencapillary recruitmentcooperativitydiffusion capacityenzyme kineticsGerman romanticismhyperbolic binding and activitypositive/negative allosteric modulators (PAMs, NAMs)positive/negative homotropic and heterotropic allosters (PHoA, NHoA, PHeA, NHeA)product and substrate inhibitionspecific cellular activity

Identifiers

PMID40665777
PMCPMC12264582

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