Evidence map›Paper›PMID 29388167›Full record

ArticleJournal of the American Society for Mass Spectrometry2018

Surface Induced Dissociation Coupled with High Resolution Mass Spectrometry Unveils Heterogeneity of a 211 kDa Multicopper Oxidase Protein Complex.

Mowei Zhou, Jing Yan, Christine A Romano, Bradley M Tebo, Vicki H Wysocki, Ljiljana Paša-Tolić

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

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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

6 authors at 3 institutions in 1 country.

Mowei ZhouEnvironmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, 3335 Innovation Blvd, Richland, WA, 99354, USA.
Jing YanDepartment of Chemistry and Biochemistry, Ohio State University, 460 W 12th Ave, Columbus, OH, 43210, USA.
Christine A RomanoDivision of Environmental and Biomolecular Systems, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, OR, 97239, USA.
Bradley M TeboDivision of Environmental and Biomolecular Systems, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, OR, 97239, USA.
Vicki H WysockiDepartment of Chemistry and Biochemistry, Ohio State University, 460 W 12th Ave, Columbus, OH, 43210, USA.
Ljiljana Paša-TolićEnvironmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, 3335 Innovation Blvd, Richland, WA, 99354, USA. ljiljana.pasatolic@pnnl.gov.
Environmental Molecular Sciences Laboratory · USOregon Health & Science University · USThe Ohio State University · US

Funding

15 Tesla Bruker solariX FTICR MSS10OD018507 · OD · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2014 to 2014
$2.0M
National Science Foundation CHE-1410688National Science Foundation DBI-1202859National Science Foundation DBI 1455654NIH HHS 1S10OD018507NIH HHS S10 OD018507
6 · The paper itself

Abstract

Manganese oxidation is an important biogeochemical process that is largely regulated by bacteria through enzymatic reactions. However, the detailed mechanism is poorly understood due to challenges in isolating and characterizing these unknown enzymes. A manganese oxidase, Mnx, from Bacillus sp. PL-12 has been successfully overexpressed in active form as a protein complex with a molecular mass of 211 kDa. We have recently used surface induced dissociation (SID) and ion mobility-mass spectrometry (IM-MS) to release and detect folded subcomplexes for determining subunit connectivity and quaternary structure. The data from the native mass spectrometry experiments led to a plausible structural model of this multicopper oxidase, which has been difficult to study by conventional structural biology methods. It was also revealed that each Mnx subunit binds a variable number of copper ions. Becasue of the heterogeneity of the protein and limited mass resolution, ambiguities in assigning some of the observed peaks remained as a barrier to fully understanding the role of metals and potential unknown ligands in Mnx. In this study, we performed SID in a modified Fourier transform-ion cyclotron resonance (FTICR) mass spectrometer. The high mass accuracy and resolution offered by FTICR unveiled unexpected artificial modifications on the protein that had been previously thought to be iron bound species based on lower resolution spectra. Additionally, isotopically resolved spectra of the released subcomplexes revealed the metal binding stoichiometry at different structural levels. This method holds great potential for in-depth characterization of metalloproteins and protein-ligand complexes. Graphical Abstract ᅟ.

Indexed as

BacillusBacterial ProteinsCopperManganese CompoundsMass SpectrometryMetalloproteinsOxidesProtein BindingBacterial ProteinsCopperManganese Compoundsmanganese oxideMetalloproteinsOxidesHigh resolution mass spectrometryMetalloproteinNative mass spectrometryProtein complexProtein–ligand interactionSurface induced dissociation

Identifiers

PMID29388167
PMCPMC7305857
OpenAlexW2787615079

What OpenQuestion holds

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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.