ArticleJournal of the American Chemical Society2014
Electron transfer control in soluble methane monooxygenase.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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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.
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Who cites it
21 citing papers in PubMed, 41 citations in OpenAlex.
- Computational Characterization of Ligand Recognition and Inhibition in a 1,4-Dioxane-Degrading Propane Monooxygenase.Journal of chemical information and modeling · 2026Article
- Cryo-EM Structures Reveal the Molecular Basis of Asymmetric Allosteric Activation by MMOB in the Hydroxylase of Soluble Methane Monooxygenase.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Structural and evolutionary insights into the isoprene monooxygenases.FEMS microbiology ecology · 2026Article
- Phylogenetic and Functional Diversity of Soluble Di-Iron Monooxygenases.Environmental microbiology · 2025Review
- A rationally designed miniature of soluble methane monooxygenase enables rapid and high-yield methanol production in Escherichia coli.Nature communications · 2024Article
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- X-ray Crystal Structures of Methane Monooxygenase Hydroxylase Complexes with Variants of Its Regulatory Component: Correlations with Altered Reaction Cycle Dynamics.Biochemistry · 2022Article
- Ferritin-Like Proteins: A Conserved Core for a Myriad of Enzyme Complexes.Sub-cellular biochemistry · 2022Article
- An Overview of the Electron-Transfer Proteins That Activate Alkane Monooxygenase (AlkB).Frontiers in microbiology · 2022Review
- Soluble Methane Monooxygenase Component Interactions Monitored byBiochemistry · 2021Article
- Biochemistry of aerobic biological methane oxidation.Chemical Society reviews · 2021Review
- MMOD-induced structural changes of hydroxylase in soluble methane monooxygenase.Science advances · 2019Article
- Evaluating apoenzyme-coenzyme-substrate interactions of methane monooxygenase with an engineered active site for electron harvesting: a computational study.Journal of molecular modeling · 2018Article
- A tale of two methane monooxygenases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Biocatalysts for methane conversion: big progress on breaking a small substrate.Current opinion in chemical biology · 2016Review
- Hydroxylation of methane through component interactions in soluble methane monooxygenases.Journal of microbiology (Seoul, Korea) · 2016Review
- Structural Basis for Oxygen Activation at a Heterodinuclear Manganese/Iron Cofactor.The Journal of biological chemistry · 2015Article
- Coupling Oxygen Consumption with Hydrocarbon Oxidation in Bacterial Multicomponent Monooxygenases.Accounts of chemical research · 2015Article
- Enzymatic oxidation of methane.Biochemistry · 2015Review
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The hydroxylation or epoxidation of hydrocarbons by bacterial multicomponent monooxygenases (BMMs) requires the interplay of three or four protein components. How component protein interactions control catalysis, however, is not well understood. In particular, the binding sites of the reductase components on the surface of their cognate hydroxylases and the role(s) that the regulatory proteins play during intermolecular electron transfer leading to the hydroxylase reduction have been enigmatic. Here we determine the reductase binding site on the hydroxylase of a BMM enzyme, soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath). We present evidence that the ferredoxin domain of the reductase binds to the canyon region of the hydroxylase, previously determined to be the regulatory protein binding site as well. The latter thus inhibits reductase binding to the hydroxylase and, consequently, intermolecular electron transfer from the reductase to the hydroxylase diiron active site. The binding competition between the regulatory protein and the reductase may serve as a control mechanism for regulating electron transfer, and other BMM enzymes are likely to adopt the same mechanism.
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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.