Evidence map›Paper›PMID 41518912›Full record

ArticleJournal of inorganic biochemistry2026

Structural basis for organism-dependent effects on spectroscopic properties of type 1 copper azurin by the same axial methionine to histidine mutation.

Jiaqing Xu, Lu Yu, Sheng-Song Yu, Yiwei Liu, Jing-Xiang Wang, Jun-Jie Li, Casey Van Stappen, Han-Qing Yu, Mark J Nilges, Yi Lu

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of inorganic biochemistry, 2026. 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

10 authors.

Jiaqing XuDepartment of Chemistry, University of Texas at Austin, 105 E. 24th St., Austin, TX 78712, United States.
Lu YuDepartment of Environmental Science and Engineering, University of Science and Technology of China, Hefei 230026, China.
Sheng-Song YuDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, United States; Department of Environmental Science and Engineering, University of Science and Technology of China, Hefei 230026, China.
Yiwei LiuDepartment of Chemistry, University of Texas at Austin, 105 E. 24th St., Austin, TX 78712, United States.
Jing-Xiang WangDepartment of Chemistry, University of Texas at Austin, 105 E. 24th St., Austin, TX 78712, United States.
Jun-Jie LiDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, United States; Key Laboratory of Laboratory Medical Diagnostics, Ministry of Education, Department of Laboratory Medicine, Chongqing Medical University, No. 1 Yi Xue Yuan Road, Chongqing 400016, China.
Casey Van StappenDepartment of Chemistry, University of Texas at Austin, 105 E. 24th St., Austin, TX 78712, United States. Electronic address: cvanstap@iu.edu.
Han-Qing YuDepartment of Environmental Science and Engineering, University of Science and Technology of China, Hefei 230026, China. Electronic address: hqyu@ustc.edu.cn.
Mark J NilgesSchool of Chemical Sciences Electron Paramagnetic Resonance Lab, University of Illinois at Urbana-Champaign, Urbana, IL 61801, United States.
Yi LuDepartment of Chemistry, University of Texas at Austin, 105 E. 24th St., Austin, TX 78712, United States; Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, United States. Electronic address: yi.lu@utexas.edu.

Funding

Design and Selection of Novel Metalloenzymes for Biocatalysis, Bioimaging, and Genetic EngineeringR35GM141931 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Yi Lu · 2021 to 2026
$3.5M
Spectroscopic and Mechanistic Characterization of Novel DNAzymes Selective for Redox-active Metal IonsF32GM145134 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI VAN STAPPEN, CASEY MICHAEL · 2022 to 2024
$233k
NIGMS NIH HHS F32 GM145134NIGMS NIH HHS R35 GM141931
6 · The paper itself

Abstract

Cupredoxins are a family of copper proteins that mediate electron transfer in key biological processes, and understanding structural features responsible for their spectroscopic properties is important for elucidating structure-function relationships. Here, we characterize the effect of mutation of the axial methionine to histidine in azurin from Pseudomonas aeruginosa (M121HAz-PA) using UV-Vis absorption, electron paramagnetic resonance (EPR) spectroscopy, and X-ray crystallography to examine how the same M121H mutation affects spectroscopic properties differently from its homolog in Alcaligenes denitrificans (M121HAz-AD). M121HAz-PA shows a pH-dependent UV-vis spectral change from pH 4 to pH 8, with unusual EPR features, indicating changes in coordination electronic structure. Azide binding titrations produce EPR spectra intermediate between type 1 copper (T1Cu) and type 2 copper (T2Cu), supporting that changes of (exogenous) ligand coordination drive significant geometric and electronic rearrangements. X-ray crystallography reveals differences in axial His121 coordination mode to Cu

Indexed as

AzurinBacterial ProteinsCopperHistidineMethionineMutationPseudomonas aeruginosaAlcaligenesCrystallography, X-RayElectron Spin Resonance SpectroscopyModels, MolecularAzurinBacterial ProteinsCopperHistidineMethionineAzurinCupredoxinLigand coordinationType 1 copper site

Identifiers

PMID41518912
PMCPMC13091565

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.