Evidence map›Paper›PMID 39891686›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2025

A semisynthetic, multicofactor artificial metalloenzyme retains independent site activity.

Ashlee E Wertz, Ilmari Rosenkampff, Philippe Ibouanga, Matthias Huber, Corinna R Hess, Olaf Rüdiger, Hannah S Shafaat

Abstract read
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In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 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. 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

7 authors.

Ashlee E WertzDepartment of Chemistry and Biochemistry, The Ohio State University, 100 W 18th Ave, Columbus, OH, 43210, USA.
Ilmari RosenkampffMax Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, 45470, Mülheim an der Ruhr, Germany.
Philippe IbouangaDepartment of Chemistry and Catalysis Research Center, Technical University of Munich, 85748, Garching, Germany.
Matthias HuberDepartment of Chemistry and Catalysis Research Center, Technical University of Munich, 85748, Garching, Germany.
Corinna R HessDepartment of Chemistry and Catalysis Research Center, Technical University of Munich, 85748, Garching, Germany.
Olaf RüdigerMax Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, 45470, Mülheim an der Ruhr, Germany. olaf.ruediger@cec.mpg.de.
Hannah S ShafaatDepartment of Chemistry and Biochemistry, The Ohio State University, 100 W 18th Ave, Columbus, OH, 43210, USA. shafaat@ucla.edu.

Funding

Deutsche Forschungsgemeinschaft 460156759National Science Foundation 2140211
6 · The paper itself

Abstract

Native metalloenzymes are unparalleled in their ability to perform efficient small molecule activation reactions, converting simple substrates into complex products. Most of these natural systems possess multiple metallocofactors to facilitate electron transfer or cascade catalysis. While the field of artificial metalloenzymes is growing at a rapid rate, examples of artificial enzymes that leverage two distinct cofactors remain scarce. In this work, we describe a new class of artificial enzymes containing two different metallocofactors, incorporated through bioorthogonal strategies. Nickel-substituted rubredoxin (Ni

Indexed as

MetalloproteinsRubredoxinsCatalytic DomainHydrogenaseModels, MolecularNickelHydrogenaseMetalloproteinsNickelRubredoxinsBioorthogonal couplingElectrocatalysisElectron transferHydrogenaseRedox cofactor

Identifiers

PMID39891686
PMCPMC11914312

What OpenQuestion holds

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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.