Evidence map›Paper›PMID 35385600›Full record

ArticleChembiochem : a European journal of chemical biology2022

Crucial Role of the Chaperonin GroES/EL for Heterologous Production of the Soluble Methane Monooxygenase from Methylomonas methanica MC09.

Domenic Zill, Elisabeth Lettau, Christian Lorent, Franziska Seifert, Praveen K Singh, Lars Lauterbach

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

7 citing papers in PubMed, 19 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.

Domenic ZillTechnische Universität Berlin, Institute for Chemistry, Straße des 17. Juni 135, 10437, Berlin, Germany.
Elisabeth LettauTechnische Universität Berlin, Institute for Chemistry, Straße des 17. Juni 135, 10437, Berlin, Germany.
Christian LorentTechnische Universität Berlin, Institute for Chemistry, Straße des 17. Juni 135, 10437, Berlin, Germany.
Franziska SeifertMartin-Luther-Universität Halle-Wittenberg, Institut für Pharmazeutische Technologie und Biopharmazie, Weinbergweg 22, 06120, Halle (Saale), Germany.
Praveen K SinghRWTH Aachen University, iAMB - Institute of Applied Microbiology, Worringer Weg 1, 52074, Aachen, Germany.
Lars LauterbachTechnische Universität Berlin, Institute for Chemistry, Straße des 17. Juni 135, 10437, Berlin, Germany.ORCID 0000-0002-6601-6473
Technische Universität Berlin · DEMartin Luther University Halle-Wittenberg · DERWTH Aachen University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methane is a widespread energy source and can serve as an attractive C1 building block for a future bioeconomy. The soluble methane monooxygenase (sMMO) is able to break the strong C-H bond of methane and convert it to methanol. The high structural complexity, multiplex cofactors, and unfamiliar folding or maturation procedures of sMMO have hampered the heterologous production and thus biotechnological applications. Here, we demonstrate the heterologous production of active sMMO from the marine Methylomonas methanica MC09 in Escherichia coli by co-synthesizing the GroES/EL chaperonin. Iron determination, electron paramagnetic resonance spectroscopy, and native gel immunoblots revealed the incorporation of the non-heme diiron centre and homodimer formation of active sMMO. The production of recombinant sMMO will enable the expansion of the possibilities of detailed studies, allowing for a variety of novel biotechnological applications.

Indexed as

Escherichia coli ProteinsMethylomonasChaperoninsEscherichia coliHeat-Shock ProteinsMethaneOxygenasesChaperoninsEscherichia coli ProteinsGroE protein, E coliHeat-Shock ProteinsMethanemethane monooxygenaseOxygenasesbiocatalysisC1green energyhydroxylasesmetalloenzymes

Identifiers

PMID35385600
PMCPMC9324122
OpenAlexW4224294126

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.