Evidence map›Paper›PMID 41047894›Full record

ArticleJournal of the American Chemical Society2025

A Post-translational Histidine-Histidine Cross-Link Enhances Enzymatic Oxygen Reduction Activity with Greater pH Adaptability.

Yiwei Liu, Avery C Vilbert, Barshali Ghosh, Robert P Young, Eric D Merkley, Arnab Mukherjee, Lisa Phan, Casey Van Stappen, Ambika Baghi-Damodaran, Kyle D Miner and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. MS-Based Proteomics Approach in Mapping Protein-Protein Interaction.Advances in experimental medicine and biology · 2026
    Review
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.

Yiwei LiuDepartment of Chemistry, University of Texas at Austin, Austin, Texas 78712, United States.ORCID 0000-0002-7899-2279
Avery C VilbertPacific Northwest National Laboratory, Richland, Washington 99354, United States.
Barshali GhoshDepartment of Chemistry, University of Texas at Austin, Austin, Texas 78712, United States.
Robert P YoungPacific Northwest National Laboratory, Richland, Washington 99354, United States.ORCID 0000-0002-2686-9594
Eric D MerkleyPacific Northwest National Laboratory, Richland, Washington 99354, United States.ORCID 0000-0002-5486-4723
Arnab MukherjeeDepartment of Chemistry, University of Illinois at Urbana-Champaign, Champaign, Illinois 61801, United States.
Lisa PhanDepartment of Chemistry, University of Texas at Austin, Austin, Texas 78712, United States.
Casey Van StappenDepartment of Chemistry, University of Texas at Austin, Austin, Texas 78712, United States.ORCID 0000-0002-1770-2231
Ambika Baghi-DamodaranDepartment of Chemistry, University of Illinois at Urbana-Champaign, Champaign, Illinois 61801, United States.ORCID 0000-0002-4901-074X
Kyle D MinerDepartment of Chemistry, University of Illinois at Urbana-Champaign, Champaign, Illinois 61801, United States.
Joshua AdkinsPacific Northwest National Laboratory, Richland, Washington 99354, United States.ORCID 0000-0003-0399-0700
John CortPacific Northwest National Laboratory, Richland, Washington 99354, United States.ORCID 0000-0001-6342-6461
Yi LuDepartment of Chemistry, University of Texas at Austin, Austin, Texas 78712, United States.ORCID 0000-0003-1221-6709

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
NIGMS NIH HHS R35 GM141931
6 · The paper itself

Abstract

Cross-linked protein residues exist as enzyme cofactors to enable or enhance catalytic activities. Despite their importance in nature, the chemical identity of the cross-links is limited to certain amino acid combinations, whose function and the formation mechanism remain insufficiently understood due to the difficulty in isolating native enzymes without the cross-links. Herein, we report the formation and characterization of both His-Tyr and His-His cross-links under oxidative enzymatic turnover conditions in L29H/F33Y/F43H Mb, a structural and functional model of heme-copper oxidase (HCO). The connectivity of the cross-link was characterized as N

Indexed as

HistidineOxidoreductasesOxygenCrystallography, X-RayHydrogen-Ion ConcentrationModels, MolecularOxidation-ReductionProtein Processing, Post-Translationalcopper oxidaseHistidineOxidoreductasesOxygen

Identifiers

PMID41047894
PMCPMC12687290

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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.