ArticleApplied and environmental microbiology2007
Mutagenesis of the "leucine gate" to explore the basis of catalytic versatility in soluble methane monooxygenase.
Article in Applied and environmental microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 52 citations in OpenAlex.
- Structural and evolutionary insights into the isoprene monooxygenases.FEMS microbiology ecology · 2026Article
- Industrial applicability of enzymatic and whole-cell processes for the utilization of C1 building blocks.Nature communications · 2025Review
- Capturing methane with recombinant soluble methane monooxygenase and recombinant methyl-coenzyme M reductase.Microbial biotechnology · 2024Review
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- Enhancement of Methane Catalysis Rates inBiomolecules · 2022Article
- Biochemistry of aerobic biological methane oxidation.Chemical Society reviews · 2021Review
- Sensitive and Rapid Phenotyping of Microbes With Soluble Methane Monooxygenase Using a Droplet-Based Assay.Frontiers in bioengineering and biotechnology · 2020Article
- Metals and Methanotrophy.Applied and environmental microbiology · 2018Review
- Recent Advances in the Genetic Manipulation of Methylosinus trichosporium OB3b.Methods in enzymology · 2018Article
- Microbial transformations of selenite by methane-oxidizing bacteria.Applied microbiology and biotechnology · 2017Article
- Mutagenesis and expression of methane monooxygenase to alter regioselectivity with aromatic substrates.FEMS microbiology letters · 2017Article
- Methanobactins: from genome to function.Metallomics : integrated biometal science · 2017Review
- Methane-Oxidizing Enzymes: An Upstream Problem in Biological Gas-to-Liquids Conversion.Journal of the American Chemical Society · 2016Review
- SmoXYB1C1Z of Mycobacterium sp. strain NBB4: a soluble methane monooxygenase (sMMO)-like enzyme, active on C2 to C4 alkanes and alkenes.Applied and environmental microbiology · 2014Article
- Engineering non-heme mono- and dioxygenases for biocatalysis.Computational and structural biotechnology journal · 2012Review
- Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex.The Journal of biological chemistry · 2011Article
- Kinetic characterization of the soluble butane monooxygenase from Thauera butanivorans, formerly 'Pseudomonas butanovora'.Microbiology (Reading, England) · 2009Article
- Molecular determinants of the regioselectivity of toluene/o-xylene monooxygenase from Pseudomonas sp. strain OX1.Applied and environmental microbiology · 2009Article
- Protein engineering of toluene monooxygenases for synthesis of chiral sulfoxides.Applied and environmental microbiology · 2008Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Soluble methane monooxygenase (sMMO) from methane-oxidizing bacteria is a multicomponent nonheme oxygenase that naturally oxidizes methane to methanol and can also cooxidize a wide range of adventitious substrates, including mono- and diaromatic hydrocarbons. Leucine 110, at the mouth of the active site in the alpha subunit of the hydroxylase component of sMMO, has been suggested to act as a gate to control the access of substrates to the active site. Previous crystallography of the wild-type sMMO has indicated at least two conformations of the enzyme that have the "leucine gate" open to different extents, and mutagenesis of homologous enzymes has indicated a role for this residue in the control of substrate range and regioselectivity with aromatic substrates. By further refinement of the system for homologous expression of sMMO that we developed previously, we have been able to prepare a range of site-directed mutations at position 110 in the alpha subunit of sMMO. All the mutants (with Gly, Cys, Arg, and Tyr, respectively, at this position) showed relaxations of regioselectivity compared to the wild type with monoaromatic substrates and biphenyl, including the appearance of new products arising from hydroxylation at the 2- and 3- positions on the benzene ring. Mutants with the larger Arg and Trp residues at position 110 also showed shifts in regioselectivity during naphthalene hydroxylation from the 2- to the 1- position. No evidence that mutagenesis of Leu 110 could allow very large substrates to enter the active site was found, however, since the mutants (like the wild type) were inactive toward the triaromatic hydrocarbons anthracene and phenanthrene. Thus, our results indicate that the "leucine gate" in sMMO is more important in controlling the precision of regioselectivity than the sizes of substrates that can enter the active site.
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