ArticleNature2013
Control of substrate access to the active site in methane monooxygenase.
Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
What it found
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Who cites it
63 citing papers in PubMed.
- 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
- Biological conversion of methane to organic molecules: towards a low-carbon bioeconomy.National science review · 2026Review
- The Heme Oxygenase-Like Diiron Enzyme HrmI Reveals Altered Regulatory Mechanisms for Dioxygen Activation and Substrate N-Oxygenation.Journal of the American Chemical Society · 2025Article
- Breaking symmetry: Metal-guided assembly of heterotrimeric coiled coils.Methods in enzymology · 2025Article
- A rationally designed miniature of soluble methane monooxygenase enables rapid and high-yield methanol production in Escherichia coli.Nature communications · 2024Article
- One-Pot Cu/SAPO-34 for Continuous Methane Selective Oxidation to Methanol.Molecules (Basel, Switzerland) · 2024Article
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- MmoD regulates soluble methane monooxygenase and methanobactin production inApplied and environmental microbiology · 2023Article
- Transcriptional regulation of soluble methane monooxygenase via enhancer-binding protein derived fromApplied and environmental microbiology · 2023Article
- Article
- Polarized Au(I)/Rh(I) bimetallic pairs cooperatively trigger ligand non-innocence and bond activation.Dalton transactions (Cambridge, England : 2003) · 2023Article
- Small molecule activation with bimetallic systems: a landscape of cooperative reactivity.Chemical communications (Cambridge, England) · 2022Review
- Crucial Role of the Chaperonin GroES/EL for Heterologous Production of the Soluble Methane Monooxygenase from Methylomonas methanica MC09.Chembiochem : a European journal of chemical biology · 2022Article
- Article
- Purification and Characterization of the Isoprene Monooxygenase fromApplied and environmental microbiology · 2022Article
- Electron Transfer to Hydroxylase through Component Interactions in Soluble Methane Monooxygenase.Journal of microbiology and biotechnology · 2022Article
- Catalytic and Spectroscopic Properties of the Halotolerant Soluble Methane Monooxygenase Reductase from Methylomonas methanica MC09.Chembiochem : a European journal of chemical biology · 2022Article
- 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
3 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Methanotrophs consume methane as their major carbon source and have an essential role in the global carbon cycle by limiting escape of this greenhouse gas to the atmosphere. These bacteria oxidize methane to methanol by soluble and particulate methane monooxygenases (MMOs). Soluble MMO contains three protein components, a 251-kilodalton hydroxylase (MMOH), a 38.6-kilodalton reductase (MMOR), and a 15.9-kilodalton regulatory protein (MMOB), required to couple electron consumption with substrate hydroxylation at the catalytic diiron centre of MMOH. Until now, the role of MMOB has remained ambiguous owing to a lack of atomic-level information about the MMOH-MMOB (hereafter termed H-B) complex. Here we remedy this deficiency by providing a crystal structure of H-B, which reveals the manner by which MMOB controls the conformation of residues in MMOH crucial for substrate access to the active site. MMOB docks at the α(2)β(2) interface of α(2)β(2)γ(2) MMOH, and triggers simultaneous conformational changes in the α-subunit that modulate oxygen and methane access as well as proton delivery to the diiron centre. Without such careful control by MMOB of these substrate routes to the diiron active site, the enzyme operates as an NADH oxidase rather than a monooxygenase. Biological catalysis involving small substrates is often accomplished in nature by large proteins and protein complexes. The structure presented in this work provides an elegant example of this principle.
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