Evidence map›Paper›PMID 41315263›Full record

ArticleNature communications2025

Structural basis of menaquinone reduction by succinate dehydrogenase from Chloroflexus aurantiacus.

Xin Zhang, Jingyi Wu, Jiamao Wang, Huimin He, Aokun Liu, Xin Hong, Yuanyi Yu, Xinkai Pei, Xianjie Fang, Yueyong Xin and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. 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

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

13 authors.

Xin Zhang *Zhejiang Key Laboratory of Medical Epigenetics, Hangzhou Normal University, Hangzhou, China.ORCID http://orcid.org/0000-0002-6734-759X
Jingyi Wu *Zhejiang Key Laboratory of Medical Epigenetics, Hangzhou Normal University, Hangzhou, China.
Jiamao WangZhejiang Key Laboratory of Medical Epigenetics, Hangzhou Normal University, Hangzhou, China.
Huimin HePhotosynthesis Research Center, College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, China.
Aokun LiuDivision of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China.
Xin HongZhejiang Key Laboratory of Medical Epigenetics, Hangzhou Normal University, Hangzhou, China.
Yuanyi YuZhejiang Key Laboratory of Medical Epigenetics, Hangzhou Normal University, Hangzhou, China.
Xinkai PeiZhejiang Key Laboratory of Medical Epigenetics, Hangzhou Normal University, Hangzhou, China.
Xianjie FangZhejiang Key Laboratory of Organosilicon Material Technology, Hangzhou Normal University, Hangzhou, China.
Yueyong XinPhotosynthesis Research Center, College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, China. yueyongxin@hznu.edu.cn.ORCID http://orcid.org/0000-0002-0252-7346
Lu YuDivision of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China. luyuesr@ustc.edu.cn.ORCID http://orcid.org/0000-0003-4852-0008
Changlin TianDivision of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China. cltian@sjtu.edu.cn.ORCID http://orcid.org/0000-0001-9315-900X
Xiaoling XuZhejiang Key Laboratory of Medical Epigenetics, Hangzhou Normal University, Hangzhou, China. xuxl@hznu.edu.cn.ORCID http://orcid.org/0000-0001-8995-1213

Funding

National Natural Science Foundation of China (National Science Foundation of China) 22437005National Natural Science Foundation of China (National Science Foundation of China) 31570738National Natural Science Foundation of China (National Science Foundation of China) 31870740Youth Innovation Promotion Association of the Chinese Academy of Sciences (Youth Innovation Promotion Association CAS) 2022455
6 · The paper itself

Abstract

Succinate: menaquinone oxidoreductase (SQR) couples the oxidation of succinate with the reduction of menaquinone (MK) as part of the TCA cycle and the aerobic respiratory chain in MK-containing bacteria and archaea. Despite its significance, questions persist regarding the electron and proton transfer mechanisms that drive the endergonic MK reduction by succinate. In this study, we determine cryo-EM structures of succinate dehydrogenase (SDH) from Chloroflexus aurantiacus (CaSDH), a facultative filamentous anoxygenic phototroph (FAP) that forms one of the earliest branches of photosynthetic bacteria. The structures of trimeric CaSDH, resolved in both apo- and MK-bound forms, reveal a single membrane-anchoring subunit containing two b-type hemes, a canonical Q

Indexed as

Bacterial ProteinsChloroflexusSuccinate DehydrogenaseVitamin K 2Cryoelectron MicroscopyElectron TransportModels, MolecularOxidation-ReductionSuccinic AcidBacterial ProteinsSuccinate DehydrogenaseSuccinic AcidVitamin K 2

Identifiers

PMID41315263
PMCPMC12663545

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.