Evidence map›Paper›PMID 39793048›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

Electron transfer in polysaccharide monooxygenase catalysis.

Richard I Sayler, William C Thomas, Alexander J Rose, Michael A Marletta

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

4 authors.

Richard I SaylerCalifornia Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720.ORCID 0000-0001-7252-707X
William C ThomasCalifornia Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720.
Alexander J RoseDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720.
Michael A MarlettaCalifornia Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720.ORCID 0000-0001-8715-4253

Funding

User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI Gregory L Hura · 2017 to 2026
$28.6M
Pilatus 6mS10OD021832 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI ADAMS, PAUL DAVID · 2016 to 2016
$980k
A Fast Pixel-Array Pilatus 2M Detector for Automated Macromolecular Crystallography Data CollectionS10OD026941 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI ADAMS, PAUL DAVID · 2019 to 2019
$563k
Structural and biochemical investigations into the mechanism and evolution of soluble guanylate cyclase regulationF32GM149060 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI THOMAS, WILLIAM CAREY · 2023 to 2024
$143k
Investigating the oxidative chemistry and electron transfer in polysaccharide monooxygenasesF32GM143897 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI SAYLER, RICHARD · 2022 to 2023
$137k
HHS | NIH (NIH) F32-GM143897HHS | NIH (NIH) F32-GM149060HHS | NIH (NIH) S10OD021832HHS | NIH (NIH) S10OD026941NIGMS NIH HHS F32 GM143897NIGMS NIH HHS F32 GM149060NIGMS NIH HHS P30 GM124169NIH HHS S10 OD021832NIH HHS S10 OD026941NSF (NSF) CHE-1904540U.S. Department of Energy (DOE) DE-AC02-05CH11231
6 · The paper itself

Abstract

Polysaccharide monooxygenase (PMO) catalysis involves the chemically difficult hydroxylation of unactivated C-H bonds in carbohydrates. The reaction requires reducing equivalents and will utilize either oxygen or hydrogen peroxide as a cosubstrate. Two key mechanistic questions are addressed here: 1) How does the enzyme regulate the timely and tightly controlled electron delivery to the mononuclear copper active site, especially when bound substrate occludes the active site? and 2) How does this electron delivery differ when utilizing oxygen or hydrogen peroxide as a cosubstrate? Using a computational approach, potential paths of electron transfer (ET) to the active site copper ion were identified in a representative AA9 family PMO from

Indexed as

Catalytic DomainCopperMixed Function OxygenasesCatalysisCrystallography, X-RayElectron TransportHydrogen PeroxideModels, MolecularMutationOxidation-ReductionOxygenPolysaccharidesSordarialesCopperHydrogen PeroxideMixed Function OxygenasesOxygenPolysaccharidescatalysiselectron transferpolysaccharide degradationpolysaccharide monooxygenase

Identifiers

PMID39793048
PMCPMC11725913

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

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 Socratic graph.