Evidence map›Paper›PMID 40991675›Full record

ArticlePLoS genetics2025

Naphthoquinone preferentially pairs with non-proton-pumping NADH dehydrogenase for respiratory electron transport.

Snehal V Khairnar, Anjali V Patil, L Karvannan, Amitesh Anand

Abstract read
In one paragraph

Article in PLoS genetics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Snehal V KhairnarDepartment of Biological Sciences, Tata Institute of Fundamental Research, Mumbai, Maharashtra, India.
Anjali V PatilDepartment of Biological Sciences, Tata Institute of Fundamental Research, Mumbai, Maharashtra, India.
L KarvannanDepartment of Biological Sciences, Tata Institute of Fundamental Research, Mumbai, Maharashtra, India.
Amitesh AnandDepartment of Biological Sciences, Tata Institute of Fundamental Research, Mumbai, Maharashtra, India.ORCID https://orcid.org/0000-0002-3720-4301

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Optimal resource allocation is crucial to bacterial physiology and necessitates strategic metabolic decisions. One such evolutionary adaptation was the shift to high-potential respiratory chains following Earth's Great Oxidation Event. Respiratory quinones, key redox-active electron carrier molecules, evolved from naphthoquinones (NQs) to ubiquinones (UQs) in response to oxygen availability. The two quinone types differ in their redox potential, with UQs possessing higher potential. Therefore, NQs are more autooxidizable and electron-leaky than UQs. Using adaptive laboratory evolution of a NQ-dependent Escherichia coli strain, we previously showed the fitness advantage of high-potential quinones. Here, we resolve a paradoxical growth benefit conferred by the loss of function of the pyruvate dehydrogenase complex regulator, revealing that NQs preferentially pair with the non-proton-pumping NADH dehydrogenase, thereby optimizing electron transport in low-potential respiratory chains under aerobic conditions.

Indexed as

NADH DehydrogenaseNaphthoquinonesElectron TransportEscherichia coliEscherichia coli ProteinsOxidation-ReductionOxygenUbiquinoneEscherichia coli ProteinsNADH DehydrogenaseNaphthoquinonesOxygenUbiquinone

Identifiers

PMID40991675
PMCPMC12510636

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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.