Matrix Control of Solvent and Electron Flow in a Nonheme Diiron Nitrite Reductase.

Hung-Ying Chen, Yi-Shan Lu, Chu-Chun Cheng, Feng-Chun Lo, Tzuhsiung Yang, Yun-Wei Chiang

Abstract read

In one paragraph

Article in JACS Au, 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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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

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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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

6 authors.

Hung-Ying ChenDepartment of Chemistry, National Tsing Hua University, Hsinchu 300-044, Taiwan.

Yi-Shan LuDepartment of Chemistry, National Tsing Hua University, Hsinchu 300-044, Taiwan.

Chu-Chun ChengDepartment of Chemistry, National Tsing Hua University, Hsinchu 300-044, Taiwan.

Feng-Chun LoDepartment of Chemistry, National Tsing Hua University, Hsinchu 300-044, Taiwan.

Tzuhsiung YangDepartment of Chemistry, National Tsing Hua University, Hsinchu 300-044, Taiwan.ORCID https://orcid.org/0000-0002-6751-9806

Yun-Wei ChiangDepartment of Chemistry, National Tsing Hua University, Hsinchu 300-044, Taiwan.ORCID https://orcid.org/0000-0002-2101-8918

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nonheme diiron enzymes catalyze a wide range of biologically essential redox transformations. Despite extensive study, how the surrounding protein matrix coordinates electron transfer, proton delivery, and solvent access and whether mechanistic insights derived

Indexed as

EPR spectroscopynitrite reductasenonheme diiron enzymesolvent gatingsolvent kinetic isotope effect

Identifiers

PMID42063837

DOI10.1021/jacsau.6c00043

PMCPMC13126187

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