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- MINIREVIEW] Hydroxylation of methane through component interactions in soluble methane monooxygenases
- Seung Jae Lee
- J. Microbiol. 2016;54(4):277-282. Published online April 1, 2016
- DOI: https://doi.org/10.1007/s12275-016-5642-6
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- 7 Crossref
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Abstract
- Methane hydroxylation through methane monooxygenases (MMOs) is a key aspect due to their control of the carbon cycle in the ecology system and recent applications of methane gas in the field of bioenergy and bioremediation. Methanotropic bacteria perform a specific microbial conversion from methane, one of the most stable carbon compounds, to methanol through elaborate mechanisms. MMOs express particulate methane monooxygenase (pMMO) in most strains and soluble methane monooxygenase (sMMO) under copper-limited conditions. The mechanisms of MMO have been widely studied from sMMO belonging to the bacterial multicomponent monooxygenase (BMM) superfamily. This enzyme has diiron active sites where different types of hydrocarbons are oxidized through orchestrated hydroxylase, regulatory and reductase components for precise control of hydrocarbons, oxygen, protons, and electrons. Recent advances in biophysical studies, including structural and enzymatic achievements for sMMO, have explained component interactions, substrate pathways, and intermediates of sMMO. In this account, oxidation of methane in sMMO is discussed with recent progress that is critical for understanding the microbial applications of C-H activation in one-carbon substrates.
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Citations
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Complete genome sequences of
Methylococcus capsulatus
(Norfolk) and
Methylocaldum szegediense
(Norfolk) isolated from a landfill methane biofilter
David Pearce, Elliot Brooks, Charles Wright, Daniel Rankin, Andrew T. Crombie, J. Colin Murrell, Elinne Becket
Microbiology Resource Announcements.2024;[Epub] CrossRef - Effect of monodentate heterocycle co-ligands on the μ-1,2-peroxo-diiron(III) mediated aldehyde deformylation reactions
Patrik Török, Dóra Lakk-Bogáth, Duenpen Unjaroen, Wesley R. Browne, József Kaizer
Journal of Inorganic Biochemistry.2024; 258: 112620. CrossRef - Crucial Role of the Chaperonin GroES/EL for Heterologous Production of the Soluble Methane Monooxygenase from Methylomonas methanica MC09
Domenic Zill, Elisabeth Lettau, Christian Lorent, Franziska Seifert, Praveen K. Singh, Lars Lauterbach
ChemBioChem.2022;[Epub] CrossRef - Bioinspired Oxidation of Methane: From Academic Models of Methane Monooxygenases to Direct Conversion of Methane to Methanol
A. A. Shteinman
Kinetics and Catalysis.2020; 61(3): 339. CrossRef - Effect of the Nuclearity and Coordination of Cu and Fe Sites in β Zeolites on the Oxidation of Hydrocarbons
Petr Sazama, Jaroslava Moravkova, Stepan Sklenak, Alena Vondrova, Edyta Tabor, Galina Sadovska, Radim Pilar
ACS Catalysis.2020; 10(7): 3984. CrossRef - Enrichment culture and identification of endophytic methanotrophs isolated from peatland plants
Zofia Stępniewska, Weronika Goraj, Agnieszka Kuźniar, Natalia Łopacka, Magdalena Małysza
Folia Microbiologica.2017; 62(5): 381. CrossRef - A growing family of O2 activating dinuclear iron enzymes with key catalytic diiron(III)-peroxo intermediates: Biological systems and chemical models
Alexandre Trehoux, Jean-Pierre Mahy, Frédéric Avenier
Coordination Chemistry Reviews.2016; 322: 142. CrossRef
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Complete genome sequences of
Methylococcus capsulatus
(Norfolk) and
Methylocaldum szegediense
(Norfolk) isolated from a landfill methane biofilter
- Role of the Amino Acid Residued in the Catalysis of Catechol 2,3-dioxygenase from Pseudomonas putida SU10 as Probed by Chemical Modification and Random Mutagenesis
- Park, Sun Jung , park, Jin Mo , Lee, Byeong Jae , Min, Kyung Hee
- J. Microbiol. 1997;35(4):300-308.
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Abstract
- The catechol 2,3-dioxygenase (C23O) encoded by the Pseudomonas putida xylE gene was over-produced in Escherichia coli and purified to homogeneity. The activity of the C23O required the reduced form of the Fe(II) ion since the enzyme was highly susceptible to inactivation with hydrogen perocide but reactivated with the addition of ferrous sulfate in conjunction with ascorbic acid. The C23O activity was abolished by treatment with the chemical reagents, diethyl-pyrocarbonate (DEPC), tetranitromethane (TNM), and 1-cyclohexy1-3-(2-morpholinoethyl) car-bodiimidemetho-ρ-toluenesulfontate (CMC), which are modifying reagents of histidine, tyrosine and glutamic acid, respectively. These results suggest that histidine, tyrosine and glutamic acid residues may be good active sites for the enzyme activity. These amino acid residues are conserved residues may be good active sites for the enzyme activity. These amino acid residues are conserved residues among several extradion dioxygenases and have the chemical potential to serveas ligands for Fe(II) coordination. Analysis of random point mutants in the C23O gene derived by PCR technique revealed that the mutated positions of two mutants, T179S and S211R, were located near the conserved His165 amd Hos217 residues, respectively. This finding indicates that these two positions, along with the conserved histidine residues, are specially effective regions for the enzyme function.
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