ReviewBiochemical Society transactions2008
The metal centres of particulate methane mono-oxygenase.
Review in Biochemical Society transactions, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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.
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.
Who cites it
14 citing papers in PubMed, 35 citations in OpenAlex.
- Critical evaluation of three cryo-EM structures of particulate methane monooxygenase by quantum refinement.Acta crystallographica. Section D, Structural biology · 2025Article
- Unraveling the Nature of Extraframework Catalytic Ensembles in Zeolites: Flexibility and Dynamics of the Copper-Oxo Trimers in Mordenite.The journal of physical chemistry letters · 2021Article
- Methane-Oxidizing Enzymes: An Upstream Problem in Biological Gas-to-Liquids Conversion.Journal of the American Chemical Society · 2016Review
- Improved Efficiency for Partial Oxidation of Methane by Controlled Copper Deposition on Surface-Modified ZSM-5.ChemCatChem · 2016Article
- Enzymatic oxidation of methane.Biochemistry · 2015Review
- Effects of zinc on particulate methane monooxygenase activity and structure.The Journal of biological chemistry · 2014Article
- Metallation and mismetallation of iron and manganese proteins in vitro and in vivo: the class I ribonucleotide reductases as a case study.Metallomics : integrated biometal science · 2012Review
- The divergent AmoC3 subunit of ammonia monooxygenase functions as part of a stress response system in Nitrosomonas europaea.Journal of bacteriology · 2012Article
- Evidence for oxygen binding at the active site of particulate methane monooxygenase.Journal of the American Chemical Society · 2012Article
- Isolation and purification of Cu-free methanobactin from Methylosinus trichosporium OB3b.Geochemical transactions · 2011Article
- Metal reconstitution of particulate methane monooxygenase and heterologous expression of the pmoB subunit.Methods in enzymology · 2011Article
- Biochemistry: Getting the metal right.Nature · 2010Article
- Article
- Architecture and active site of particulate methane monooxygenase.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
pMMO (particulate methane mono-oxygenase) is an integral membrane metalloenzyme that catalyses the oxidation of methane to methanol. The pMMO metal active site has not been identified, precluding detailed investigation of the reaction mechanism. Models for the metal centres proposed by various research groups have evolved as crystallographic and spectroscopic data have become available. The present review traces the evolution of these active-site models before and after the 2005 Methylococcus capsulatus (Bath) pMMO crystal structure determination.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.