Evidence map›Paper›PMID 31591267›Full record

ArticleThe Journal of biological chemistry2019

Chemical flexibility of heterobimetallic Mn/Fe cofactors: R2lox and R2c proteins.

Yury Kutin, Ramona Kositzki, Rui M M Branca, Vivek Srinivas, Daniel Lundin, Michael Haumann, Martin Högbom, Nicholas Cox, Julia J Griese

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.5field-weighted citation impact, top 39% of its field
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

11 citing papers in PubMed, 17 citations in OpenAlex.

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  10. The Bacillus anthracis class Ib ribonucleotide reductase subunit NrdF intrinsically selects manganese over iron.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
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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

9 authors at 6 institutions in 3 countries.

Yury KutinMax Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany.
Ramona KositzkiInstitut für Experimentalphysik, Freie Universität Berlin, D-14195 Berlin, Germany.
Rui M M BrancaCancer Proteomics Mass Spectrometry, Department of Oncology-Pathology, Science for Life Laboratory, Karolinska Institute, Box 1031, SE-171 21 Solna, Sweden.
Vivek SrinivasDepartment of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Daniel LundinDepartment of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Michael HaumannInstitut für Experimentalphysik, Freie Universität Berlin, D-14195 Berlin, Germany.
Martin HögbomDepartment of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Nicholas CoxResearch School of Chemistry, Australian National University, Canberra, Australian Capital Territory 2601, Australia. Electronic address: nick.cox@anu.edu.au.
Julia J GrieseDepartment of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden; Department of Cell and Molecular Biology, Uppsala University, SE-751 24 Uppsala, Sweden. Electronic address: julia.griese@icm.uu.se.
Stockholm University · SEFreie Universität Berlin · DEAustralian National University · AUMax Planck Institute for Chemical Energy Conversion · DEScience for Life Laboratory · SEUppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A heterobimetallic Mn/Fe cofactor is present in the R2 subunit of class Ic ribonucleotide reductases (R2c) and in R2-like ligand-binding oxidases (R2lox). Although the protein-derived metal ligands are the same in both groups of proteins, the connectivity of the two metal ions and the chemistry each cofactor performs are different: in R2c, a one-electron oxidant, the Mn/Fe dimer is linked by two oxygen bridges (μ-oxo/μ-hydroxo), whereas in R2lox, a two-electron oxidant, it is linked by a single oxygen bridge (μ-hydroxo) and a fatty acid ligand. Here, we identified a second coordination sphere residue that directs the divergent reactivity of the protein scaffold. We found that the residue that directly precedes the N-terminal carboxylate metal ligand is conserved as a glycine within the R2lox group but not in R2c. Substitution of the glycine with leucine converted the resting-state R2lox cofactor to an R2c-like cofactor, a μ-oxo/μ-hydroxo-bridged Mn

Indexed as

Bacterial ProteinsCatalytic DomainCrystallography, X-RayElectron Spin Resonance SpectroscopyGeobacillusIronLigandsManganeseModels, MolecularMolecular StructureMutationOxidation-ReductionOxidoreductasesOxygenProtein DomainsRibonucleotide ReductasesBacterial ProteinsIronLigandsManganeseOxidoreductasesOxygenRibonucleotide Reductasesbinuclear metal cofactorelectron paramagnetic resonance (EPR)ferritinmass spectrometry (MS)metalloproteinR2-like ligand-binding oxidaseredox chemistryribonucleotide reductaseX-ray absorption spectroscopyX-ray crystallography

Identifiers

PMID31591267
PMCPMC6885639
OpenAlexW2980181826

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.