Evidence map›Paper›PMID 42489679›Full record

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

Molecular strategies for flux control in an electron bifurcation protein.

Niven Singh, Kiriko Terai, David Beratan

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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. 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.

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

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

3 authors.

Niven SinghProgram in Computational Biology and Bioinformatics, Duke University, Durham, NC, 27710, USA.
Kiriko TeraiDepartment of Chemistry, Duke University, Durham, NC, 27708, USA.
David BeratanProgram in Computational Biology and Bioinformatics, Duke University, Durham, NC, 27710, USA. david.beratan@duke.edu.

Funding

Basic Energy Sciences DE-SC0021144U.S. Department of Energy DE-SC0021144
6 · The paper itself

Abstract

Electron-bifurcating flavoproteins split electron pairs and deposit them in spatially separated electron-acceptor pools. Just how electron-transfer networks regulate steady-state electron-bifurcation (EB) fluxes and efficiencies remains unclear. We model the steady-state kinetics of electron-bifurcation in NADH-dependent ferredoxin-NADP[Formula: see text] oxidoreductase I (Nfn1), based on the protein's structure and electrochemistry. We use a many-particle master-equation to simulate the steady-state kinetics. The analysis identifies control points that are defined by electronic couplings between cofactors, and we explore how the interactions between cofactors influence EB function. We find that couplings on the low-potential branch dictate EB efficiency and the onset of short-circuiting, while the couplings on the high-potential branch determine the magnitude of the steady-state bifurcation flux in Nfn1. Analysis of interactions using the tunneling pathway model indicates that pathway connectivity between the bifurcating donor and its high-potential acceptor is weak for its distance; this decoupling may serve to further suppress short-circuiting and favor productive electron flow.

Indexed as

ElectronsElectron TransportKineticsNADNADDonor-acceptor interactionsElectron bifurcationElectron transferSteady-state kineticsTunneling pathways

Identifiers

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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.