Author

Wei Peng

Shandong UniversityORCID 0000-0002-4085-5842Unclaimed ORCID profile · follow to get notified of new preprints

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Wei Peng3 papers · Qinghai University

Biology Disciplines

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Biophysics· 1 Molecular Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:bacteria (other)· 1 Assay:cryo-EM· 1 Assay:imaging· 1 Organism:multiple species· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1

Frequent Co-Authors

Shengying LiiD· 2 shared Tieqiang Mao· 2 shared Zhi-Cong He· 2 shared Zongqiang LiiD· 2 shared Chuanlun ZhangiD· 1 shared Guoping ZhaoiD· 1 shared Hongpo DongiD· 1 shared Jiawen YangiD· 1 shared

Activity by Year

2026-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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2 shared papersBiophysics

Shengying LiORCID

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2 papers

Recent·Most cited

Catalytic and inhibitory architecture of comammox ammonia monooxygenase

Zongqiang Li, Tieqiang Mao, Xiaoyun Yang, Zhi-Cong He, Jiawen Yang, Rihui Wu, Kmy Leung, Shengying Li, Ping Han, Wei Peng

This study reports cryo-EM structures of comammox AMO from Nitrospira inopinata and identifies its catalytic and inhibitor-responsive architecture, revealing a methyl-PQ-linked mechanism and stress response to nitrification inhibitors.

bioRxiv · Sep 5, 2026 · PreprintBiophysics

Structural basis for catalytic and inhibitory divergence between archaeal and bacterial ammonia monooxygenases

Xiaoyun Yang, Tieqiang Mao, Zhi-Cong He, Yan Chen, Guoping Zhao, Peng Jin, Shengying Li, Hongpo Dong, Wei Peng, Chuanlun Zhang, Zongqiang Li

Archaeal ammonia monooxygenase (AMO) is a cup-shaped homotrimer using a mononuclear CuD site; inhibitors bind bacterial AMO's dicopper center directly but apparently inactivate archaeal AMO indirectly by relocating copper.

bioRxiv · Sep 1, 2026 · PreprintMolecular Biology✦ In-depth digest