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Recovery of particulate methane monooxygenase structure and activity in a lipid bilayer.

Koo CW, Tucci FJ, He Y, Rosenzweig AC
Science 375 1287-1291 (2022)
Related entries: 7s4h, 7s4i, 7s4j, 7s4k, 7s4l, 7t4o, 7t4p

Cited: 21 times
EuropePMC logo PMID: 35298269

Abstract

Bacterial methane oxidation using the enzyme particulate methane monooxygenase (pMMO) contributes to the removal of environmental methane, a potent greenhouse gas. Crystal structures determined using inactive, detergent-solubilized pMMO lack several conserved regions neighboring the proposed active site. We show that reconstituting pMMO in nanodiscs with lipids extracted from the native organism restores methane oxidation activity. Multiple nanodisc-embedded pMMO structures determined by cryo-electron microscopy to 2.14- to 2.46-angstrom resolution reveal the structure of pMMO in a lipid environment. The resulting model includes stabilizing lipids, regions of the PmoA and PmoC subunits not observed in prior structures, and a previously undetected copper-binding site in the PmoC subunit with an adjacent hydrophobic cavity. These structures provide a revised framework for understanding and engineering pMMO function.

Reviews - 7s4m mentioned but not cited (1)

  1. Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases. Tucci FJ, Rosenzweig AC. Chem Rev 124 1288-1320 (2024)

Articles - 7s4m mentioned but not cited (1)

  1. Distance-based global analysis of consistent cis-bonds in protein backbones. Okada T, Tomoike F. Heliyon 9 e18598 (2023)


Reviews citing this publication (5)

  1. Methane Oxidation to Methanol. Dummer NF, Willock DJ, He Q, Howard MJ, Lewis RJ, Qi G, Taylor SH, Xu J, Bethell D, Kiely CJ, Hutchings GJ. Chem Rev 123 6359-6411 (2023)
  2. The histidine brace: nature's copper alternative to haem? Walton PH, Davies GJ, Diaz DE, Franco-Cairo JP. FEBS Lett 597 485-494 (2023)
  3. Nitrification and beyond: metabolic versatility of ammonia oxidising archaea. Wright CL, Lehtovirta-Morley LE. ISME J 17 1358-1368 (2023)
  4. Orchestrating copper binding: structure and variations on the cupredoxin fold. Guo J, Fisher OS. J Biol Inorg Chem 27 529-540 (2022)
  5. Characterization of Protein-Membrane Interactions in Yeast Autophagy. Leary KA, Ragusa MJ. Cells 11 1876 (2022)

Articles citing this publication (14)

  1. Unexpected complexity of the ammonia monooxygenase in archaea. Hodgskiss LH, Melcher M, Kerou M, Chen W, Ponce-Toledo RI, Savvides SN, Wienkoop S, Hartl M, Schleper C. ISME J 17 588-599 (2023)
  2. Structure and activity of particulate methane monooxygenase arrays in methanotrophs. Zhu Y, Koo CW, Cassidy CK, Spink MC, Ni T, Zanetti-Domingues LC, Bateman B, Martin-Fernandez ML, Shen J, Sheng Y, Song Y, Yang Z, Rosenzweig AC, Zhang P. Nat Commun 13 5221 (2022)
  3. Kβ X-ray Emission Spectroscopy of Cu(I)-Lytic Polysaccharide Monooxygenase: Direct Observation of the Frontier Molecular Orbital for H2O2 Activation. Lim H, Brueggemeyer MT, Transue WJ, Meier KK, Jones SM, Kroll T, Sokaras D, Kelemen B, Hedman B, Hodgson KO, Solomon EI. J Am Chem Soc 145 16015-16025 (2023)
  4. A Conserved Second Sphere Residue Tunes Copper Site Reactivity in Lytic Polysaccharide Monooxygenases. Hall KR, Joseph C, Ayuso-Fernández I, Tamhankar A, Rieder L, Skaali R, Golten O, Neese F, Røhr ÅK, Jannuzzi SAV, DeBeer S, Eijsink VGH, Sørlie M. J Am Chem Soc 145 18888-18903 (2023)
  5. Cell-Free Protein Synthesis of Particulate Methane Monooxygenase into Nanodiscs. Koo CW, Hershewe JM, Jewett MC, Rosenzweig AC. ACS Synth Biol 11 4009-4017 (2022)
  6. Enzymatic Hydroxylation of Aliphatic C-H Bonds by a Mn/Fe Cofactor. Powell MM, Rao G, Britt RD, Rittle J. J Am Chem Soc 145 16526-16537 (2023)
  7. Product analog binding identifies the copper active site of particulate methane monooxygenase. Tucci FJ, Jodts RJ, Hoffman BM, Rosenzweig AC. Nat Catal 6 1194-1204 (2023)
  8. A Copper Cage-Complex as Mimic of the pMMO CuC Site. Bete SC, May LK, Woite P, Roemelt M, Otte M. Angew Chem Int Ed Engl 61 e202206120 (2022)
  9. Methane Activation by a Mononuclear Copper Active Site in the Zeolite Mordenite: Effect of Metal Nuclearity on Reactivity. Heyer AJ, Plessers D, Braun A, Rhoda HM, Bols ML, Hedman B, Hodgson KO, Schoonheydt RA, Sels BF, Solomon EI. J Am Chem Soc 144 19305-19316 (2022)
  10. Recombinant expression and subcellular targeting of the particulate methane monooxygenase (pMMO) protein components in plants. Spatola Rossi T, Tolmie AF, Nichol T, Pain C, Harrison P, Smith TJ, Fricker M, Kriechbaumer V. Sci Rep 13 15337 (2023)
  11. A designed Copper Histidine-brace enzyme for oxidative depolymerization of polysaccharides as a model of lytic polysaccharide monooxygenase. Liu Y, Harnden KA, Van Stappen C, Dikanov SA, Lu Y. Proc Natl Acad Sci U S A 120 e2308286120 (2023)
  12. Concluding remarks: discussion on natural and artificial enzymes including synthetic models. Karlin KD, Hota PK, Kim B. Faraday Discuss 234 388-404 (2022)
  13. Determination of the iron(IV) local spin states of the Q intermediate of soluble methane monooxygenase by Kβ X-ray emission spectroscopy. Cutsail GE, Banerjee R, Rice DB, McCubbin Stepanic O, Lipscomb JD, DeBeer S. J Biol Inorg Chem 27 573-582 (2022)
  14. MmoD regulates soluble methane monooxygenase and methanobactin production in Methylosinus trichosporium OB3b. Peng P, Yang J, DiSpirito AA, Semrau JD. Appl Environ Microbiol 89 e0160123 (2023)


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