Roles of Subunit ND2/NuoN in the Proton Pumping Coupling Mechanism of Complex I.

Andrew E Wadley, Madhavan Narayanan, Eiko Nakamaru-Ogiso

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In one paragraph

Article in International journal of molecular sciences, 2026. 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

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.

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2 · The registry

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Andrew E WadleyJohnson Research Foundation, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.

Madhavan NarayananJohnson Research Foundation, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.ORCID 0000-0001-5700-6962

Eiko Nakamaru-OgisoJohnson Research Foundation, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.

Funding

Proton pumping mechanism in complex IR01GM097409 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OGISO, EIKO · 2011 to 2015

$1.5M

NIHGMS R01GM097409

6 · The paper itself

Abstract

Complex I (NADH:quinone oxidoreductase, CI) is central to cellular aerobic energy metabolism. The L-shaped structure of CI is unique, where the hydrophilic arm is responsible for the electron transfer function and the membrane arm operates proton pumping. These two functional sites are spatially far apart yet functionally connected. This basic core subunit architecture is highly conserved from bacterial to mammalian CI. Here, to gain detailed mechanistic insight into the role of the membrane subunit ND2 in the coupling mechanism, we mutated several highly conserved residues in the middle of the membrane axis of NuoN, the

Indexed as

Electron Transport Complex IEscherichia coliEscherichia coli ProteinsNADH DehydrogenaseProton PumpsElectron TransportMutationProtein SubunitsElectron Transport Complex IEscherichia coli ProteinsNADH DehydrogenaseProtein SubunitsProton PumpsCIenergy couplingND2proton pumpingubiquinone

Identifiers

PMID41977177

DOI10.3390/ijms27072990

PMCPMC13073174

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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.