Evidence map›Paper›PMID 41968187›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2026

The evolutionary footprint of histidine in hemoglobin and myoglobin: an implication towards their function.

Jayraj Biswas, Kauseki Dutta, Kakali Biswas, Raja Banerjee

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Jayraj BiswasDepartment of Biotechnology, Maulana Abul Kalam Azad University of Technology,WB, Haringhata, 741249, West Bengal, India.
Kauseki DuttaDepartment of Biotechnology, Maulana Abul Kalam Azad University of Technology,WB, Haringhata, 741249, West Bengal, India.
Kakali BiswasDepartment of Biotechnology, Maulana Abul Kalam Azad University of Technology,WB, Haringhata, 741249, West Bengal, India.
Raja BanerjeeDepartment of Biotechnology, Maulana Abul Kalam Azad University of Technology,WB, Haringhata, 741249, West Bengal, India. banraja10@gmail.com.ORCID http://orcid.org/0000-0003-1890-6401

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hemoglobin and myoglobin are essential oxygen-binding proteins whose structural integrity is critical for proper function. This study performs atomic-level comparisons of wild-type and mutant forms to investigate how specific mutations impact oxygen-binding affinity. Substitution of the proximal histidine, responsible for coordinating the iron atom in the heme group, with tyrosine results shortening of bond distances in haemoglobin, while Van der Waals clashes in myoglobin; impairing function of both. Other mutations (α125Leu > Pro, β34Val > Asp, β63His > Tyr, β92His > Asn) compromise the protein stability by disrupting inter-chain hydrogen bonds and helical structures, reducing oxygen-binding efficiency. Cross-species comparisons, from Actinopterygii to Mammalia, underscore strong conservation of these critical residues essential for preserving the indispensable structural and functional integrity of these proteins since the dawn of their existence.

Indexed as

Evolution, MolecularHemoglobinsHistidineMyoglobinAnimalsHumansModels, MolecularMutationOxygenHemoglobinsHistidineMyoglobinOxygenConservation of sequence &structureEvolutionHemoglobinHistidineMutationMyoglobin

Identifiers

PMID41968187

What OpenQuestion holds

Textmetadata
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.