Evidence map›Paper›PMID 40005181›Full record

ArticleMolecules (Basel, Switzerland)2025

Bond Valence Sum Parameters for Analyzing Pyranopterin Tungsten Enzyme Structures.

Jesse Lepluart, Martin L Kirk

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

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5 · Who and what money

Authors and funding

2 authors.

Jesse LepluartDepartment of Chemistry and Chemical Biology, The University of New Mexico, MSC03 2060, 1 University of New Mexico, Albuquerque, NM 87131, USA.
Martin L KirkDepartment of Chemistry and Chemical Biology, The University of New Mexico, MSC03 2060, 1 University of New Mexico, Albuquerque, NM 87131, USA.ORCID 0000-0002-1479-3318

Funding

Spectroscopic Studies of Molybdoenzymes & ModelsR01GM057378 · NIGMS · UNIVERSITY OF NEW MEXICO · PI MARTIN L KIRK · 1998 to 2026
$6.9M
NIGMS NIH HHS R01 GM057378NIH HHS GM-057378
6 · The paper itself

Abstract

The determination of tungsten oxidation states and W-ligand bond lengths for pyranopterin tungsten enzymes can be negatively impacted by Fourier series termination effects and photodamage/photoreduction in the X-ray beam. As a result, a new set of bond valence sum (BVS) parameters have been derived from bond length data on W(+4) and W(+6) model compounds that were obtained from X-ray crystallography. These new W enzyme-specific BVS parameters have been used in the analysis of pyranopterin tungsten enzyme structural data. The results of this analysis indicate that there are potential issues with the enzyme crystal structures, including the number of ligating atoms to the tungsten atom, the W-ligand bond lengths, and the W oxidation state. We conclude that a BVS analysis of crystallographic and EXAFS structural data will help address these issues, and EXAFS should be more routinely employed in the determination of pyranopterin tungsten enzyme active site structures due to the increased accuracy of this technique for the determination of W-ligand bond distances.

Indexed as

EnzymesPterinsTungstenCatalytic DomainCrystallography, X-RayLigandsModels, MolecularOxidation-ReductionEnzymesLigandsPterinspyranopterinTungstenbond valence sumdithioleneEXAFSmolybdenum enzymespyranopterintungsten enzymesX-ray crystallography

Identifiers

PMID40005181
PMCPMC11858030

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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.