Evidence map›Paper›PMID 38629782›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2024

Secondary Structure in Enzyme-Inspired Polymer Catalysts Impacts Water Oxidation Efficiency.

Graziela C Sedenho, Steffane Q Nascimento, Marjon Zamani, Frank N Crespilho, Ariel L Furst

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Genetic Surfaceome E. coli Reprogramming Enables Selective Water Oxidation.Advanced materials (Deerfield Beach, Fla.) · 2025
    Article
  2. Review
  3. Article
  4. Secondary Structure in Enzyme-Inspired Polymer Catalysts Impacts Water Oxidation Efficiency.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
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

5 authors.

Graziela C SedenhoSão Carlos Institute of Chemistry, University of São Paulo (USP), São Carlos, SP, 13566-590, Brazil.
Steffane Q NascimentoSão Carlos Institute of Chemistry, University of São Paulo (USP), São Carlos, SP, 13566-590, Brazil.
Marjon ZamaniDepartment of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA.
Frank N CrespilhoSão Carlos Institute of Chemistry, University of São Paulo (USP), São Carlos, SP, 13566-590, Brazil.
Ariel L FurstDepartment of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA.ORCID 0000-0001-9583-9703

Funding

The MIT Superfund Research Program: A Systems Approach for the Protection of Human Health from Hazardous ChemicalsP42ES027707 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI Desiree Plata · 2017 to 2026
$22.2M
TRAINING GRANTS IN ENVIROMENTAL TOXICOLOGYT32ES007020 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ESSIGMANN, JOHN M · 1985 to 2024
$13.1M
Army Research OfficeCAPESCIFAR Azrieli Global Scholars FoundationFAPESP 2018/22214-6FAPESP 2020/04796-8FAPESP 2021/10307-2FAPESP 88887.513539/2020-00NIEHSNIEHS NIH HHS P42 ES027707NIEHS NIH HHS T32 ES007020NIEHS NIH HHS Y02 ES007020
6 · The paper itself

Abstract

Protein structure plays an essential role on their stability, functionality, and catalytic activity. In this work, the interplay between the β-sheet structure and its catalytic implications to the design of enzyme-inspired materials is investigated. Here, inspiration is drawn from the active sites and β-sheet rich structure of the highly efficient multicopper oxidase (MCO) to engineer a bio-inspired electrocatalyst for water oxidation utilizing the abundant metal, copper. Copper ions are coordinated to poly-histidine (polyCuHis), as they are in MCO active sites. The resultant polyCuHis material effectively promotes water oxidation with low overpotentials (0.15 V) in alkaline systems. This activity is due to the 3D structure of the poly-histidine backbone. By increasing the prevalence of β-sheet structure and decreasing the random coil nature of the polyCuHis secondary structures, this study is able to modulates the electrocatalytic activity of this material is modulated, shifting it toward water oxidation. These results highlight the crucial role of the local environment at catalytic sites for efficient, energy-relevant transformations. Moreover, this work highlights the importance of conformational structure in the design of scaffolds for high-performance electrocatalysts.

Indexed as

Oxidation-ReductionWaterCatalysisCopperHistidineOxidoreductasesPolymersProtein Structure, SecondaryCopperHistidineOxidoreductasespolyhistidinePolymersWaterbioinspired catalystcopper complexmulticopper oxidasespoly‐histidinewater oxidation

Identifiers

PMID38629782
PMCPMC11220705

What OpenQuestion holds

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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.