Evidence map›Paper›PMID 20410881›Full record

ArticleNature2010

Oxidation of methane by a biological dicopper centre.

Ramakrishnan Balasubramanian, Stephen M Smith, Swati Rawat, Liliya A Yatsunyk, Timothy L Stemmler, Amy C Rosenzweig

Open access · greenAbstract read
In one paragraph

Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 131 papers.

0numbers the graph read from it
0cells of the map it votes in
131citing papers in PubMed
18.5field-weighted citation impact, top 1% 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

131 citing papers in PubMed, 539 citations in OpenAlex.

  1. Article
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    Review
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  20. Article

71 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Ramakrishnan BalasubramanianDepartment of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.
Stephen M Smith
Swati Rawat
Liliya A Yatsunyk
Timothy L Stemmler
Amy C Rosenzweig
Institute of Molecular and Cell Biology · RUNorthwestern University · USWayne State University · US

Funding

Particulate Methane MonooxygenaseR01GM070473 · NIGMS · NORTHWESTERN UNIVERSITY · PI ROSENZWEIG, AMY C. · 2004 to 2015
$3.7M
Structural Insights into the Function of FrataxinR01DK068139 · NIDDK · WAYNE STATE UNIVERSITY · PI STEMMLER, TIMOTHY LOUIS · 2005 to 2015
$3.5M
NIDDK NIH HHS DK068139NIDDK NIH HHS R01 DK068139NIGMS NIH HHS GM070473NIGMS NIH HHS R01 GM070473
6 · The paper itself

Abstract

Vast world reserves of methane gas are underutilized as a feedstock for the production of liquid fuels and chemicals owing to the lack of economical and sustainable strategies for the selective oxidation of methane to methanol. Current processes to activate the strong C-H bond (104 kcal mol(-1)) in methane require high temperatures, are costly and inefficient, and produce waste. In nature, methanotrophic bacteria perform this reaction under ambient conditions using metalloenzymes called methane monooxygenases (MMOs). MMOs thus provide the optimal model for an efficient, environmentally sound catalyst. There are two types of MMO. Soluble MMO (sMMO) is expressed by several strains of methanotroph under copper-limited conditions and oxidizes methane with a well-characterized catalytic di-iron centre. Particulate MMO (pMMO) is an integral membrane metalloenzyme produced by all methanotrophs and is composed of three subunits, pmoA, pmoB and pmoC, arranged in a trimeric alpha(3)beta(3)gamma(3) complex. Despite 20 years of research and the availability of two crystal structures, the metal composition and location of the pMMO metal active site are not known. Here we show that pMMO activity is dependent on copper, not iron, and that the copper active site is located in the soluble domains of the pmoB subunit rather than within the membrane. Recombinant soluble fragments of pmoB (spmoB) bind copper and have propylene and methane oxidation activities. Disruption of each copper centre in spmoB by mutagenesis indicates that the active site is a dicopper centre. These findings help resolve the pMMO controversy and provide a promising new approach to developing environmentally friendly C-H oxidation catalysts.

Indexed as

Models, MolecularCatalytic DomainCopperMethaneMethanolMethylococcus capsulatusMethylosinus trichosporiumMutationOxidation-ReductionOxygenasesProtein Structure, TertiaryCopperMethanemethane monooxygenaseMethanolOxygenases

Identifiers

PMID20410881
PMCPMC2999467
OpenAlexW2074023228

What OpenQuestion holds

Textmetadata
LicenceTDM
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.