Probing anion recognition in a cobalt(II) de novo designed metalloprotein.

Salvatore La Gatta, Jacob K Firby, James E Penner-Hahn, Vincent L Pecoraro

Abstract read

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

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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

4 authors.

Salvatore La GattaDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.

Jacob K FirbyDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.

James E Penner-HahnDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA; Department of Biophysics, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: jeph@umich.edu.

Vincent L PecoraroDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: vlpec@umich.edu.

Funding

Designing Functional Metalloproteins-Equipment SupplementR01GM141086 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PECORARO, VINCENT L · 2021 to 2024

$1.3M

NIGMS NIH HHS R01 GM141086

6 · The paper itself

Abstract

Anions such as halides and pseudohalides influence metal-site structure and function. De novo designed metallocoiled coils offer a defined platform for studying how metal centers recognize small anions within an α-helical scaffold. Spectroscopic examination of anion binding to three-stranded coiled coils (3SCCs) using artificial cobalt(II) substituted carbonic anhydrases (CA) is used as an analogue of the zinc(II) center. Scaffolds composed of three equivalents of GRW-H (Ac-GWKALEEKLKALEEKLKALEEKLKALEEKHKALEEKG-NH

Indexed as

CobaltMetalloproteinsAnionsCarbonic AnhydrasesModels, MolecularThiocyanatesX-Ray Absorption SpectroscopyAnionsCarbonic AnhydrasesCobaltMetalloproteinsthiocyanateThiocyanatesAnion bindingCobalt(II) coordination chemistryDe novo designed metalloproteinsThree-stranded coiled coil

Identifiers

PMID41712971

DOI10.1016/j.jinorgbio.2026.113268

PMCPMC13262294

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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.