Evidence map›Paper›PMID 19286415›Full record

ReviewCurrent opinion in chemical biology2009

Copper-dioxygen complex mediated C-H bond oxygenation: relevance for particulate methane monooxygenase (pMMO).

Richard A Himes, Kenneth D Karlin

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
11.2field-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

49 citing papers in PubMed, 221 citations in OpenAlex.

  1. Review
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  8. Reactivity of a stable copper-dioxygen complex.Chemical communications (Cambridge, England) · 2017
    Article
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  10. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Richard A HimesDepartment of Chemistry, The Johns Hopkins University, Baltimore, MD 21218, United States. rhimes1@jhu.edu
Kenneth D Karlin
Johns Hopkins University · US

Funding

NEW COPPER(I) CHEMISTRY-MODELS FOR METALLOPROTEINSR01GM028962 · NIGMS · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI KARLIN, KENNETH D. · 1985 to 2020
$6.7M
BIOINORGANIC COPPER COORDINATION CHEMISTRYR37GM028962 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI KARLIN, KENNETH D. · 1993 to 2002
$882k
Copper-peptide Chemistry;Alzheimer's Disease RelevanceF32AG026923 · NIA · JOHNS HOPKINS UNIVERSITY · PI HIMES, RICHARD A · 2005 to 2007
$135k
NIA NIH HHS F32 AG026923NIGMS NIH HHS GM 28962NIGMS NIH HHS R01 GM028962NIGMS NIH HHS R37 GM028962
6 · The paper itself

Abstract

Particulate methane monooxygenase (pMMO), an integral membrane protein found in methanotrophic bacteria, catalyzes the oxidation of methane to methanol. Expression and greater activity of the enzyme in the presence of copper ion suggest that pMMO is a cuprous metalloenzyme. Recent advances - especially the first crystal structures of pMMO - have energized the field, but the nature of the active site(s) and the mechanism of methane oxidation remain poorly understood-yet hotly contested. Herein the authors briefly review the current understanding of the pMMO metal sites and discuss advances in small molecule Cu-O(2) chemistry that may contribute to an understanding of copper-ion mediated hydrocarbon oxidation chemistry.

Indexed as

Bacterial ProteinsCatalytic DomainCopperCrystallography, X-RayMethaneOxidation-ReductionOxygenOxygenasesBacterial ProteinsCopperMethanemethane monooxygenaseOxygenOxygenases

Identifiers

PMID19286415
PMCPMC2676220
OpenAlexW1991374426

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.