Evidence map›Paper›PMID 22725967›Full record

ReviewCritical reviews in biochemistry and molecular biology

Architecture and active site of particulate methane monooxygenase.

Megen A Culpepper, Amy C Rosenzweig

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

47 citing papers in PubMed, 143 citations in OpenAlex.

  1. HChemistry (Weinheim an der Bergstrasse, Germany) · 2026
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  6. Determination of the iron(IV) local spin states of the Q intermediate of soluble methane monooxygenase by Kβ X-ray emission spectroscopy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
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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

2 authors at 1 institution in 1 country.

Megen A CulpepperDepartments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, IL 60208, USA.
Amy C Rosenzweig
Northwestern University · US

Funding

Particulate Methane MonooxygenaseR01GM070473 · NIGMS · NORTHWESTERN UNIVERSITY · PI ROSENZWEIG, AMY C. · 2004 to 2015
$3.7M
Elucidating the mechanism of particulate methane monooxygenaseF32GM097049 · NIGMS · NORTHWESTERN UNIVERSITY · PI CULPEPPER, MEGEN A · 2011 to 2013
$155k
NIGMS NIH HHS F32 GM097049NIGMS NIH HHS F32GM097049NIGMS NIH HHS GM070473NIGMS NIH HHS R01 GM070473
6 · The paper itself

Abstract

Particulate methane monooxygenase (pMMO) is an integral membrane metalloenzyme that oxidizes methane to methanol in methanotrophic bacteria, organisms that live on methane gas as their sole carbon source. Understanding pMMO function has important implications for bioremediation applications and for the development of new, environmentally friendly catalysts for the direct conversion of methane to methanol. Crystal structures of pMMOs from three different methanotrophs reveal a trimeric architecture, consisting of three copies each of the pmoB, pmoA, and pmoC subunits. There are three distinct metal centers in each protomer of the trimer, mononuclear and dinuclear copper sites in the periplasmic regions of pmoB and a mononuclear site within the membrane that can be occupied by copper or zinc. Various models for the pMMO active site have been proposed within these structural constraints, including dicopper, tricopper, and diiron centers. Biochemical and spectroscopic data on pMMO and recombinant soluble fragments, denoted spmoB proteins, indicate that the active site involves copper and is located at the site of the dicopper center in the pmoB subunit. Initial spectroscopic evidence for O(2) binding at this site has been obtained. Despite these findings, questions remain about the active site identity and nuclearity and will be the focus of future studies.

Indexed as

CatalysisCatalytic DomainCopperMetalsMethaneMethanolModels, MolecularOxygenOxygenasesProtein ConformationZincCopperMetalsMethanemethane monooxygenaseMethanolOxygenOxygenasesZinc

Identifiers

PMID22725967
PMCPMC3474877
OpenAlexW2050749384

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.