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Annual Review of Biochemistry

Volume 88, 2019

Soluble Methane Monooxygenase

Abstract

Aerobic life is possible because the molecular structure of oxygen (O) makes direct reaction with most organic materials at ambient temperatures an exceptionally slow process. Of course, these reactions are inherently very favorable, and they occur rapidly with the release of a great deal of energy at high temperature. Nature has been able to tap this sequestered reservoir of energy with great spatial and temporal selectivity at ambient temperatures through the evolution of oxidase and oxygenase enzymes. One mechanism used by these enzymes for O activation has been studied in detail for the soluble form of the enzyme methane monooxygenase. These studies have revealed the step-by-step process of O activation and insertion into the ultimately stable C–H bond of methane. Additionally, an elegant regulatory mechanism has been defined that enlists size selection and quantum tunneling to allow methane oxidation to occur specifically in the presence of more easily oxidized substrates.

Keyword(s): crystallography, kinetics, methane, monooxygenase, oxygen activation, spectroscopy
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2019-06-20
2024-04-19
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Literature Cited

  1. 1. 
    Hanson RS, Hanson TE. 1996. Methanotrophic bacteria. Microbiol. Rev. 60:439–47
     [Google Scholar]
  2. 2. 
    Chistoserdova L, Gomelsky L, Vorholt JA, Gomelsky M, Tsygankov YD, Lidstrom ME 2000. Analysis of two formaldehyde oxidation pathways in Methylobacillus flagellatus KT, a ribulose monophosphate cycle methylotroph. Microbiology 146:233–38
     [Google Scholar]
  3. 3. 
    Sirajuddin S, Rosenzweig AC. 2015. Enzymatic oxidation of methane. Biochemistry 54:2283–94
     [Google Scholar]
  4. 4. 
    Colby J, Stirling DI, Dalton H 1977. The soluble methane monooxygenase of Methylococcus capsulatus (Bath): Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic, and heterocyclic compounds. Biochem. J. 165:395–402
     [Google Scholar]
  5. 5. 
    Wallar BJ, Lipscomb JD. 1996. Dioxygen activation by enzymes containing binuclear non-heme iron clusters. Chem. Rev. 96:2625–57
     [Google Scholar]
  6. 6. 
    Banerjee R, Komor AJ, Lipscomb JD 2017. Use of isotopes and isotope effects for investigations of diiron oxygenase mechanisms. Meth. Enzymol. 596:239–90
     [Google Scholar]
  7. 7. 
    Tinberg CE, Lippard SJ. 2011. Dioxygen activation in soluble methane monooxygenase. Acc. Chem. Res. 44:280–88
     [Google Scholar]
  8. 8. 
    Fox BG, Froland WA, Dege JE, Lipscomb JD 1989. Methane monooxygenase from Methylosinus trichosporium OB3b. Purification and properties of a three-component system with high specific activity from a type II methanotroph. J. Biol. Chem. 264:10023–33
     [Google Scholar]
  9. 9. 
    Pilkington SJ, Dalton H. 1990. Soluble methane monooxygenase from Methylococcus capsulatus (Bath). Methods Enzymol 188:181–90
     [Google Scholar]
  10. 10. 
    Baik M-H, Newcomb M, Friesner RA, Lippard SJ 2003. Mechanistic studies on the hydroxylation of methane by methane monooxygenase. Chem. Rev. 103:2385–419
     [Google Scholar]
  11. 11. 
    Rosenzweig AC, Frederick CA, Lippard SJ, Nordlund P 1993. Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. Nature 366:537–43
     [Google Scholar]
  12. 12. 
    Rosenzweig AC, Nordlund P, Takahara PM, Frederick CA, Lippard SJ 1995. Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states. Chem. Biol. 2:409–18
     [Google Scholar]
  13. 13. 
    Rosenzweig AC, Brandstetter H, Whittington DA, Nordlund P, Lippard SJ, Frederick CA 1997. Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions. Proteins 29:141–52
     [Google Scholar]
  14. 14. 
    Elango N, Radhakrishnan R, Froland WA, Wallar BJ, Earhart CA et al. 1997. Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b. Protein Sci 6:556–68
     [Google Scholar]
  15. 15. 
    Whittington DA, Lippard SJ. 2001. Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site. J. Am. Chem. Soc. 123:827–38
     [Google Scholar]
  16. 16. 
    Whittington DA, Sazinsky MH, Lippard SJ 2001. X-ray crystal structure of alcohol products bound at the active site of soluble methane monooxygenase hydroxylase. J. Am. Chem. Soc. 123:1794–95
     [Google Scholar]
  17. 17. 
    Whittington DA, Rosenzweig AC, Frederick CA, Lippard SJ 2001. Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase. Biochemistry 40:3476–82
     [Google Scholar]
  18. 18. 
    Chang SL, Wallar BJ, Lipscomb JD, Mayo KH 1999. Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling. Biochemistry 38:5799–812
     [Google Scholar]
  19. 19. 
    Walters KJ, Gassner GT, Lippard SJ, Wagner G 1999. Structure of the soluble methane monooxygenase regulatory protein B. PNAS 96:7877–82
     [Google Scholar]
  20. 20. 
    Chang SL, Wallar BJ, Lipscomb JD, Mayo KH 2001. Residues in Methylosinus trichosporium OB3b methane monooxygenase component B involved in molecular interactions with reduced- and oxidized-hydroxylase component: a role for the N-terminus. Biochemistry 40:9539–51
     [Google Scholar]
  21. 21. 
    Muller J, Lugovskoy AA, Wagner G, Lippard SJ 2002. NMR structure of the [2Fe-2S] ferredoxin domain from soluble methane monooxygenase reductase and interaction with its hydroxylase. Biochemistry 41:42–51
     [Google Scholar]
  22. 22. 
    Chatwood LL, Mueller J, Gross JD, Wagner G, Lippard SJ 2004. NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath). Biochemistry 43:11983–91
     [Google Scholar]
  23. 23. 
    Sazinsky MH, Merkx M, Cadieux E, Tang S, Lippard SJ 2004. Preparation and X-ray structures of metal-free, dicobalt and dimanganese forms of soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath). Biochemistry 43:16263–76
     [Google Scholar]
  24. 24. 
    Sazinsky MH, Lippard SJ. 2005. Product bound structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): protein motion in the α-subunit. J. Am. Chem. Soc. 127:5814–25
     [Google Scholar]
  25. 25. 
    Stenkamp RE. 1994. Dioxygen and hemerythrin. Chem. Rev. 94:715–26
     [Google Scholar]
  26. 26. 
    Jasniewski AJ, Que L 2018. Dioxygen activation by nonheme diiron enzymes: diverse dioxygen adducts, high-valent intermediates, and related model complexes. Chem. Rev. 118:2554–92
     [Google Scholar]
  27. 27. 
    Fox BG, Surerus KK, Münck E, Lipscomb JD 1988. Evidence for a μ-oxo-bridged binuclear iron cluster in the hydroxylase component of methane monooxygenase: Mössbauer and EPR studies. J. Biol. Chem. 263:10553–56
     [Google Scholar]
  28. 28. 
    Colby J, Dalton H. 1978. Resolution of the methane monooxygenase of Methylococcus capsulatus (Bath) into three components. Biochem. J. 171:461–68
     [Google Scholar]
  29. 29. 
    Lund J, Woodland MP, Dalton H 1985. Electron transfer reactions in the soluble methane monooxygenase of Methylococcus capsulatus (Bath). Eur. J. Biochem. 147:297–305
     [Google Scholar]
  30. 30. 
    Fox BG, Liu Y, Dege JE, Lipscomb JD 1991. Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b: identification of sites of component interaction. J. Biol. Chem. 266:540–50
     [Google Scholar]
  31. 31. 
    Liu Y, Nesheim JC, Paulsen KE, Stankovich MT, Lipscomb JD 1997. Roles of the methane monooxygenase reductase component in the regulation of catalysis. Biochemistry 36:5223–33
     [Google Scholar]
  32. 32. 
    Kopp DA, Berg EA, Costello CE, Lippard SJ 2003. Structural features of covalently cross-linked hydroxylase and reductase proteins of soluble methane monooxygenase as revealed by mass spectrometric analysis. J. Biol. Chem. 278:20939–45
     [Google Scholar]
  33. 33. 
    Green J, Dalton H. 1985. Protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath): a novel regulatory protein of enzyme activity. J. Biol. Chem. 260:15795–801
     [Google Scholar]
  34. 34. 
    Froland WA, Andersson KK, Lee S-K, Liu Y, Lipscomb JD 1992. Methane monooxygenase component B and reductase alter the regioselectivity of the hydroxylase component-catalyzed reactions: a novel role for protein-protein interactions in an oxygenase mechanism. J. Biol. Chem. 267:17588–97
     [Google Scholar]
  35. 35. 
    MacArthur R, Sazinsky MH, Kuehne H, Whittington DA, Lippard SJ, Brudvig GW 2002. Component B binding to the soluble methane monooxygenase hydroxylase by saturation-recovery EPR spectroscopy of spin-labeled MMOB. J. Am. Chem. Soc. 124:13392–93
     [Google Scholar]
  36. 36. 
    Lee SJ, McCormick MS, Lippard SJ, Cho U-S 2013. Control of substrate access to the active site in methane monooxygenase. Nature 494:380–84
     [Google Scholar]
  37. 37. 
    Sazinsky MH, Dunten PW, McCormick MS, DiDonato A, Lippard SJ 2006. X-ray structure of a hydroxylase-regulatory protein complex from a hydrocarbon-oxidizing multicomponent monooxygenase, Pseudomonas sp. OX1 phenol hydroxylase. Biochemistry 45:15392–404
     [Google Scholar]
  38. 38. 
    McCormick MS, Sazinsky MH, Condon KL, Lippard SJ 2006. X-ray crystal structures of manganese(II)-reconstituted and native toluene/o-xylene monooxygenase hydroxylase reveal rotamer shifts in conserved residues and an enhanced view of the protein interior. J. Am. Chem. Soc. 128:15108–10
     [Google Scholar]
  39. 39. 
    Bailey LJ, McCoy JG, Phillips GN, Fox BG 2008. Structural consequences of effector protein complex formation in a diiron hydroxylase. PNAS 105:19194–98
     [Google Scholar]
  40. 40. 
    Liang AD, Wrobel AT, Lippard SJ 2014. A flexible glutamine regulates the catalytic activity of toluene o-xylene monooxygenase. Biochemistry 53:3585–92
     [Google Scholar]
  41. 41. 
    Sazinsky MH, Lippard SJ. 2015. Methane monooxygenase: functionalizing methane at iron and copper. Met. Ions Life Sci. 15:205–56
     [Google Scholar]
  42. 42. 
    Lee SK, Nesheim JC, Lipscomb JD 1993. Transient intermediates of the methane monooxygenase catalytic cycle. J. Biol. Chem. 268:21569–77
     [Google Scholar]
  43. 43. 
    Liu Y, Nesheim JC, Lee S-K, Lipscomb JD 1995. Gating effects of component B on oxygen activation by the methane monooxygenase hydroxylase component. J. Biol. Chem. 270:24662–65
     [Google Scholar]
  44. 44. 
    Wang W, Lippard SJ. 2014. Diiron oxidation state control of substrate access to the active site of soluble methane monooxygenase mediated by the regulatory component. J. Am. Chem. Soc. 136:2244–47
     [Google Scholar]
  45. 45. 
    Wallar BJ, Lipscomb JD. 2001. Methane monooxygenase component B mutants alter the kinetics of steps throughout the catalytic cycle. Biochemistry 40:2220–33
     [Google Scholar]
  46. 46. 
    Zhang J, Lipscomb JD. 2006. Role of the C-terminal region of the B component of Methylosinus trichosporium OB3b methane monooxygenase in the regulation of oxygen activation. Biochemistry 45:1459–69
     [Google Scholar]
  47. 47. 
    Liu KE, Valentine AM, Wang DL, Huynh BH, Edmondson DE et al. 1995. Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methylococcus capsulatus (Bath). J. Am. Chem. Soc. 117:10174–85
     [Google Scholar]
  48. 48. 
    Lee SK, Lipscomb JD. 1999. Oxygen activation catalyzed by methane monooxygenase hydroxylase component: proton delivery during the O–O bond cleavage steps. Biochemistry 38:4423–32
     [Google Scholar]
  49. 49. 
    Brazeau BJ, Lipscomb JD. 2000. Kinetics and activation thermodynamics of methane monooxygenase compound Q formation and reaction with substrates. Biochemistry 39:13503–15
     [Google Scholar]
  50. 50. 
    Tinberg CE, Lippard SJ. 2009. Revisiting the mechanism of dioxygen activation in soluble methane monooxygenase from M. capsulatus (Bath): evidence for a multi-step, proton-dependent reaction pathway. Biochemistry 48:12145–58
     [Google Scholar]
  51. 51. 
    Banerjee R, Meier KK, Münck E, Lipscomb JD 2013. Intermediate P* from soluble methane monooxygenase contains a diferrous cluster. Biochemistry 52:4331–42
     [Google Scholar]
  52. 52. 
    Hendrich MP, Münck E, Fox BG, Lipscomb JD 1990. Integer-spin EPR studies of the fully reduced methane monooxygenase hydroxylase component. J. Am. Chem. Soc. 112:5861–65
     [Google Scholar]
  53. 53. 
    Priestley ND, Floss HG, Froland WA, Lipscomb JD, Williams PG, Morimoto H 1992. Cryptic stereospecificity of methane monooxygenase. J. Am. Chem. Soc. 114:7561–62
     [Google Scholar]
  54. 54. 
    Jin Y, Lipscomb JD. 2000. Mechanistic insights into C–H activation from radical clock chemistry: oxidation of substituted methylcyclopropanes catalyzed by soluble methane monooxygenase from Methylosinus trichosporium OB3b. Biochim. Biophys. Acta 1543:47–59
     [Google Scholar]
  55. 55. 
    Brazeau BJ, Austin RN, Tarr C, Groves JT, Lipscomb JD 2001. Intermediate Q from soluble methane monooxygenase hydroxylates the mechanistic substrate probe norcarane: evidence for a stepwise reaction. J. Am. Chem. Soc. 123:11831–37
     [Google Scholar]
  56. 56. 
    Beauvais LG, Lippard SJ. 2005. Reactions of the peroxo intermediate of soluble methane monooxygenase hydroxylase with ethers. J. Am. Chem. Soc. 127:7370–78
     [Google Scholar]
  57. 57. 
    Tinberg CE, Lippard SJ. 2010. Oxidation reactions performed by soluble methane monooxygenase hydroxylase intermediates Hperoxo and Q proceed by distinct mechanisms. Biochemistry 49:7902–12
     [Google Scholar]
  58. 58. 
    Do LH, Hayashi T, Moenne-Loccoz P, Lippard SJ 2010. Carboxylate as the protonation site in (peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins. J. Am. Chem. Soc. 132:1273–75
     [Google Scholar]
  59. 59. 
    Banerjee R, Proshlyakov Y, Lipscomb JD, Proshlyakov DA 2015. Structure of the key species in the enzymatic oxidation of methane to methanol. Nature 518:431–34
     [Google Scholar]
  60. 60. 
    Lee SK, Fox BG, Froland WA, Lipscomb JD, Münck E 1993. A transient intermediate of the methane monooxygenase catalytic cycle containing a FeIVFeIV cluster. J. Am. Chem. Soc. 115:6450–51
     [Google Scholar]
  61. 61. 
    Valentine AM, Tavares P, Pereira AS, Davydov R, Krebs C et al. 1998. Generation of a mixed-valent Fe(III)Fe(IV) form of intermediate Q in the reaction cycle of soluble methane monooxygenase, an analog of intermediate X in ribonucleotide reductase R2 assembly. J. Am. Chem. Soc. 120:2190–91
     [Google Scholar]
  62. 62. 
    Wilkinson EC, Dong YH, Zang Y, Fujii H, Fraczkiewicz R et al. 1998. Raman signature of the Fe2O2 “diamond” core. J. Am. Chem. Soc. 120:955–62
     [Google Scholar]
  63. 63. 
    Nesheim JC, Lipscomb JD. 1996. Large isotope effects in methane oxidation catalyzed by methane monooxygenase: evidence for C−H bond cleavage in a reaction cycle intermediate. Biochemistry 35:10240–47
     [Google Scholar]
  64. 64. 
    Shu L, Nesheim JC, Kauffmann K, Münck E, Lipscomb JD, Que L 1997. An FeIV2O2 diamond core structure for the key intermediate Q of methane monooxygenase. Science 275:515–18
     [Google Scholar]
  65. 65. 
    Rohde J-U, In J-H, Lim M-H, Brennessel WW, Bukowski MR et al. 2003. Crystallographic and spectroscopic characterization of a nonheme Fe(IV) = O complex. Science 299:1037–39
     [Google Scholar]
  66. 66. 
    Castillo RG, Banerjee R, Allpress CJ, Rohde GT, Bill E et al. 2017. High-energy-resolution fluorescence-detected X-ray absorption of the Q intermediate of soluble methane monooxygenase. J. Am. Chem. Soc. 139:18024–33
     [Google Scholar]
  67. 67. 
    Cutsail GE, Banerjee R, Zhou A, Que L, Lipscomb JD, DeBeer S 2018. High-resolution extended X-ray absorption fine structure analysis provides evidence for a longer Fe…Fe distance in the Q intermediate of methane monooxygenase. J. Am. Chem. Soc. 140:16807–20
     [Google Scholar]
  68. 68. 
    Xue G, De Hont R, Münck E, Que L 2010. Million-fold activation of the [Fe2(μ-O)2] diamond core for C=H bond cleavage. Nat. Chem. 2:400–5
     [Google Scholar]
  69. 69. 
    Siegbahn PEM, Crabtree RH. 1997. Mechanism of C–H activation by diiron methane monooxygenases: quantum chemical studies. J. Am. Chem. Soc. 119:3103–13
     [Google Scholar]
  70. 70. 
    Siegbahn PEM. 2001. O−O bond cleavage and alkane hydroxylation in methane monooxygenase. J. Biol. Inorg. Chem. 6:27–45
     [Google Scholar]
  71. 71. 
    Mai BK, Kim Y. 2013. Theoretical studies for large tunneling and the hydrogen-transfer mechanism in the C–H activation of CH3CN by the di(μ-oxo)diiron(IV) complex: a model for intermediate Q in soluble methane monooxygenase. Chem. Eur. J. 19:3568–72
     [Google Scholar]
  72. 72. 
    Basch H, Musaev DG, Mogi K, Morokima K 2001. Theoretical studies on the mechanism of the methane → methanol conversion reaction catalyzed by methane monooxygenase (MMO): the O-side versus N-side mechanisms. J. Phys. Chem. A 105:3615–22
     [Google Scholar]
  73. 73. 
    Gherman BF, Dunietz BD, Whittington DA, Lippard SJ, Friesner RA 2001. Activation of the C–H bond of methane by intermediate Q of methane monooxygenase: a theoretical study. J. Am. Chem. Soc. 123:3836–37
     [Google Scholar]
  74. 74. 
    Musaev DG, Basch H, Morokuma K 2002. Theoretical study of the mechanism of alkane hydroxylation and ethylene epoxidation reactions catalyzed by diiron bis-oxo complexes: the effect of substrate molecules. J. Am. Chem. Soc. 124:4135–48
     [Google Scholar]
  75. 75. 
    Yoshizawa K. 2000. Two-step concerted mechanism for methane hydroxylation on the diiron active site of soluble methane monooxygenase. J. Inorg. Biochem. 78:23–34
     [Google Scholar]
  76. 76. 
    Yoshizawa K. 2006. Nonradical mechanism for methane hydroxylation by iron-oxo complexes. Acc. Chem. Res. 39:375–82
     [Google Scholar]
  77. 77. 
    Newcomb M, Le Tadic-Biadatti M-H, Chestney DL, Roberts ES, Hollenberg PF 1995. A nonsynchronous concerted mechanism for cytochrome P-450 catalyzed hydroxylation. J. Am. Chem. Soc. 117:12085–91
     [Google Scholar]
  78. 78. 
    Shestakov AF, Shilov AE. 1996. Five-coordinate carbon hydroxylation mechanism. J. Mol. Catal. A 105:1–7
     [Google Scholar]
  79. 79. 
    Gherman BF, Lippard SJ, Friesner RA 2005. Substrate hydroxylation in methane monooxygenase: quantitative modeling via mixed quantum mechanics/molecular mechanics techniques. J. Am. Chem. Soc. 127:1025–37
     [Google Scholar]
  80. 80. 
    Fox BG, Borneman JG, Wackett LP, Lipscomb JD 1990. Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b: mechanistic and environmental implications. Biochemistry 29:6419–27
     [Google Scholar]
  81. 81. 
    Groves JT. 1985. Key elements of the chemistry of cytochrome P-450. The oxygen rebound mechanism. J. Chem. Educ. 62:928–31
     [Google Scholar]
  82. 82. 
    Groves JT. 2006. High-valent iron in chemical and biological oxidations. J. Inorg. Biochem. 100:434–47
     [Google Scholar]
  83. 83. 
    Valentine AM, Wilkinson B, Liu KE, Komarpanicucci S, Priestley ND et al. 1997. Tritiated chiral alkanes as substrates for soluble methane monooxygenase from Methylococcus capsulatus (Bath): probes for the mechanism of hydroxylation. J. Am. Chem. Soc. 119:1818–27
     [Google Scholar]
  84. 84. 
    Baik M-H, Gherman BF, Friesner RA, Lippard SJ 2002. Hydroxylation of methane by non-heme diiron enzymes: molecular orbital analysis of C–H bond activation by reactive intermediate Q. J. Am. Chem. Soc. 124:14608–15
     [Google Scholar]
  85. 85. 
    Guallar V, Gherman BF, Miller WH, Lippard SJ, Friesner RA 2002. Dynamics of alkane hydroxylation at the non-heme diiron center in methane monooxygenase. J. Am. Chem. Soc. 124:3377–84
     [Google Scholar]
  86. 86. 
    Choi S-Y, Eaton PE, Kopp DA, Lippard SJ, Newcomb M, Shen R 1999. Cationic species can be produced in soluble methane monooxygenase-catalyzed hydroxylation reactions; radical intermediates are not formed. J. Am. Chem. Soc. 121:12198–99
     [Google Scholar]
  87. 87. 
    Jin Y, Lipscomb JD. 1999. Probing the mechanism of C–H activation: oxidation of methylcubane by soluble methane monooxygenase from Methylosinus trichosporium OB3b. Biochemistry 38:6178–86
     [Google Scholar]
  88. 88. 
    Valentine AM, LeTadic-Biadatti M-H, Toy PH, Newcomb M, Lippard SJ 1999. Oxidation of ultrafast radical clock substrate probes by the soluble methane monooxygenase from Methylococcus capsulatus (Bath). J. Biol. Chem. 274:10771–76
     [Google Scholar]
  89. 89. 
    Valentine AM, Stahl SS, Lippard SJ 1999. Mechanistic studies of the reaction of reduced methane monooxygenase hydroxylase with dioxygen and substrates. J. Am. Chem. Soc. 121:3876–87
     [Google Scholar]
  90. 90. 
    Brazeau BJ, Wallar BJ, Lipscomb JD 2001. Unmasking of deuterium kinetic isotope effects on the methane monooxygenase compound Q reaction by site-directed mutagenesis of component B. J. Am. Chem. Soc. 123:10421–22
     [Google Scholar]
  91. 91. 
    Klinman JP. 2006. The role of tunneling in enzyme catalysis of C–H activation. Biochim. Biophys. Acta Bioenerg. 1757:981–87
     [Google Scholar]
  92. 92. 
    Zheng H, Lipscomb JD. 2006. Regulation of methane monooxygenase catalysis based on size exclusion and quantum tunneling. Biochemistry 45:1685–92
     [Google Scholar]
  93. 93. 
    Carr CAM, Klinman JP. 2014. Hydrogen tunneling in a prokaryotic lipoxygenase. Biochemistry 53:2212–14
     [Google Scholar]
  94. 94. 
    Siebrand W, Smedarchina Z. 2006. Mechanism of CH-bond cleavage catalyzed by enzymes. Isotope Effects in Chemistry and Biology A Kohen, H-H Limbach 725–41 Boca Raton, FL: Taylor & Francis
     [Google Scholar]
  95. 95. 
    Arciero DM, Lipscomb JD. 1986. Binding of 17O-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex: evidence for direct substrate binding to the active site Fe2+ of extradiol dioxygenases. J. Biol. Chem. 261:2170–78
     [Google Scholar]
  96. 96. 
    Wolfe MD, Parales JV, Gibson DT, Lipscomb JD 2001. Single turnover chemistry and regulation of O2 activation by the oxygenase component of naphthalene 1,2-dioxygenase. J. Biol. Chem. 276:1945–53
     [Google Scholar]
  97. 97. 
    Lipscomb JD, Sligar SG, Namtvedt MJ, Gunsalus IC 1976. Autooxidation and hydroxylation reactions of oxygenated cytochrome P450cam. J. Biol. Chem. 251:1116–24
     [Google Scholar]
  98. 98. 
    Poulos TL. 2014. Heme enzyme structure and function. Chem. Rev. 114:3919–62
     [Google Scholar]
  99. 99. 
    Pau MYM, Lipscomb JD, Solomon EI 2007. Substrate activation for O2 reactions by oxidized metal centers in biology. PNAS 104:18355–62
     [Google Scholar]
  100. 100. 
    Rivard BS, Rogers MS, Marell DJ, Neibergall MB, Chakrabarty S et al. 2015. Rate-determining attack on substrate precedes Rieske cluster oxidation during cis-dihydroxylation by benzoate dioxygenase. Biochemistry 54:4652–64
     [Google Scholar]
  101. 101. 
    Komor AJ, Rivard BS, Fan R, Guo Y, Que L, Lipscomb JD 2017. CmlI N-oxygenase catalyzes the final three steps in chloramphenicol biosynthesis without dissociation of intermediates. Biochemistry 56:4940–50
     [Google Scholar]
  102. 102. 
    Sutherlin KD, Rivard BS, Bottger LH, Liu LV, Rogers MS et al. 2018. NRVS studies of the peroxide shunt intermediate in a Rieske dioxygenase and its relation to the native Fe(II) O2 reaction. J. Am. Chem. Soc. 140:5544–59
     [Google Scholar]
  103. 103. 
    Mitić N, Schwartz JK, Brazeau BJ, Lipscomb JD, Solomon EI 2008. CD and MCD studies of the effects of component B variant binding on the biferrous active site of methane monooxygenase. Biochemistry 47:8386–97
     [Google Scholar]
  104. 104. 
    Rinaldo D, Philipp DM, Lippard SJ, Friesner RA 2007. Intermediates in dioxygen activation by methane monooxygenase: a QM/MM study. J. Am. Chem. Soc. 129:3135–47
     [Google Scholar]
  105. 105. 
    Brazeau BJ, Wallar BJ, Lipscomb JD 2003. Effector proteins from P450cam and methane monooxygenase: lessons in tuning nature's powerful reagents. Biochem. Biophys. Res. Commun. 312:143–48
     [Google Scholar]
  106. 106. 
    Zhang J, Wallar BJ, Popescu CV, Renner DB, Thomas DD, Lipscomb JD 2006. Methane monooxygenase hydroxylase and B component interactions. Biochemistry 45:2913–26
     [Google Scholar]
  107. 107. 
    Brazeau BJ, Lipscomb JD. 2003. Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B. Biochemistry 42:5618–31
     [Google Scholar]
  108. 108. 
    Wang W, Liang AD, Lippard SJ 2015. Coupling oxygen consumption with hydrocarbon oxidation in bacterial multicomponent monooxygenases. Acc. Chem. Res. 48:2632–39
     [Google Scholar]
  109. 109. 
    Song WJ, Gucinski G, Sazinsky MH, Lippard SJ 2011. Tracking a defined route for O2 migration in a dioxygen-activating diiron enzyme. PNAS 108:14795–800
     [Google Scholar]
  110. 110. 
    Smith TJ, Slade SE, Burton NP, Murrell JC, Dalton H 2002. Improved system for protein engineering of the hydroxylase component of soluble methane monooxygenase. Appl. Environ. Microbiol. 68:5265–73
     [Google Scholar]
  111. 111. 
    Puri AW, Owen S, Chu F, Chavkin T, Beck DAC et al. 2015. Genetic tools for the industrially promising methanotroph Methylomicrobium buryatense. Appl. Environ. . Microbiol 81:1775–81
     [Google Scholar]
  112. 112. 
    Yan X, Chu F, Puri AW, Fu Y, Lidstrom ME 2016. Electroporation-based genetic manipulation in type I methanotrophs. Appl. Environ. Microbiol. 82:2062–69
     [Google Scholar]
  113. 113. 
    Nagel ZD, Klinman JP. 2006. Tunneling and dynamics in enzymatic hydride transfer. Chem. Rev. 106:3095–118
     [Google Scholar]
  114. 114. 
    Brandstetter H, Whittington DA, Lippard SJ, Frederick CA 1999. Mutational and structural analyses of the regulatory protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath). Chem. Biol. 6:441–49
     [Google Scholar]
  115. 115. 
    Gassner GT, Lippard SJ. 1999. Component interactions in the soluble methane monooxygenase system from Methylococcus capsulatus (Bath). Biochemistry 38:12768–85
     [Google Scholar]
  116. 116. 
    Wang W, Iacob RE, Luoh RP, Engen JR, Lippard SJ 2014. Electron transfer control in soluble methane monooxygenase. J. Am. Chem. Soc. 136:9754–62
     [Google Scholar]
  117. 117. 
    Paulsen KE, Liu Y, Fox BG, Lipscomb JD, Münck E, Stankovich MT 1994. Oxidation-reduction potentials of the methane monooxygenase hydroxylase component from Methylosinus trichosporium OB3b. Biochemistry 33:713–22
     [Google Scholar]
  118. 118. 
    Liu KE, Lippard SJ. 1991. Redox properties of the hydroxylase component of methane monooxygenase from Methylococcus capsulatus (Bath): effects of protein B, reductase, and substrate. J. Biol. Chem 266:12836–39 Erratum. 1991 J. Biol. Chem 266:24859
     [Google Scholar]
  119. 119. 
    Blazyk JL, Gassner GT, Lippard SJ 2005. Intermolecular electron-transfer reactions in soluble methane monooxygenase: a role for hysteresis in protein function. J. Am. Chem. Soc. 127:17364–76
     [Google Scholar]
  120. 120. 
    Friedle S, Reisner E, Lippard SJ 2010. Current challenges of modeling diiron enzyme active sites for dioxygen activation by biomimetic synthetic complexes. Chem. Soc. Rev. 39:2768–79
     [Google Scholar]
  121. 121. 
    Karlin KD, Lippard SJ, Valentine JS, Burrows CJ 2015. Solving 21st century problems in biological inorganic chemistry using synthetic models. Acc. Chem. Res. 48:2659–60
     [Google Scholar]
/content/journals/10.1146/annurev-biochem-013118-111529
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Soluble Methane Monooxygenase
Annual Review of Biochemistry 88, 409 (2019); https://doi.org/10.1146/annurev-biochem-013118-111529
/content/journals/10.1146/annurev-biochem-013118-111529
/content/journals/10.1146/annurev-biochem-013118-111529
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