48
2 Selective Production of Methanol …
39. Valentine AM, Wilkinson B, Liu KE, Komar-Panicucci S, Priestley ND, Williams PG, Morimoto H, Floss HG, Lippard SJ (1997) Tritiated chiral alkanes as substrates for soluble
methane monooxygenase from Methylococcus capsulatus (Bath): probes for the mechanism
of hydroxylation. J Am Chem Soc 119:1818–1827
40. Ruzicka F, Huang DS, Donnelly MI, Frey PA (1990) Methane monooxygenase catalyzed oxygenation of 1,1-dimethylcyclopropane. Evidence for radical and carbocationic intermediates.
Biochemistry 29:1696–1700
41. Choi SY, Eaton PE, Hollenberg PF, Liu KE, Lippard SJ, Newcomb M, Putt DA, Upadhyaya
SP, Xiong Y (1996) Regiochemical variations in reactions of methylcubane with tert-butoxyl
radical, cytochrome P-450 enzymes, and a methane monooxygenase system. J Am Chem Soc
118:6547–6555
42. Liu KE, Johnson CC, Newcomb M, Lippard SJ (1993) Radical clock substrate probes
and kinetic isotope effect studies of the hydroxylation of hydrocarbons by methane
monooxygenase. J Am Chem Soc 115:939–947
43. Valentine AM, LeTadic-Biadatti MH, 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 274:10771–10776
44. Wilkins PC, Dalton H, Samuel CJ, Green J (1994) Further evidence for multiple pathways in
soluble methane-monooxygenase-catalysed oxidations from the measurement of deuterium
kinetic isotope effects. Eur J Biochem 226:555–560
45. Stahl SS, Francisco WA, Merkx M, Klinman JP, Lippard SJ (2001) Oxygen kinetic isotope
effects in soluble methane monooxygenase. J Biol Chem 276:4549–4553
46. 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 48:12145–12158
47. Yoshizawa K, Yumura T (2003) A non-radical mechanism for methane hydroxylation at the
diiron active site of soluble methane monooxygenase. Chemistry 9:2347–2358
48. Mai BK, Kim Y (2014) Substrate-dependent H/D kinetic isotope effects and the role of the
di(μ-oxo)diiron(IV) core in soluble methane monooxygenase: a theoretical study. Chemistry
20:6532–6541
49. 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
50. Xue G, Pokutsa A, Que L Jr (2011) Substrate-triggered activation of a synthetic [Fe 2 (μ-O) 2 ]
diamond core for C-H bond cleavage. J Am Chem Soc 133:16657–16667
51. Saito T, Shoji M, Isobe H, Yamanaka S, Kitagawa Y, Yamada S, Kawakami T, Okumura M,
Yamaguchi K (2010) Theory of chemical bonds in metalloenzymes. XIV. Correspondence
between magnetic coupling mode and radical coupling mechanism in hydroxylations with
methane monooxygenase and related species. Int J Quant Chem 110:2955–2981
52. Tinberg CE, Lippard SJ (2011) Dioxygen activation in soluble methane monooxygenase. Acc
Chem Res 44:280–288
53. Banerjee R, Jones JC, Lipscomb JD (2019) Soluble methane monooxygenase. Annu Rev
Biochem 88:409–431
54. 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 40:3476–3482
55. 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
123:1794–1795
56. 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 127:5814–5825
57. McCormick MS, Lippard SJ (2011) Analysis of substrate access to active sites in bacterial
multicomponent monooxygenase hydroxylases: X-ray crystal structure of xenon-pressurized
phenol hydroxylase from Pseudomonas sp. OX1. Biochemistry 50:11058–11069
2 Selective Production of Methanol …
39. Valentine AM, Wilkinson B, Liu KE, Komar-Panicucci S, Priestley ND, Williams PG, Morimoto H, Floss HG, Lippard SJ (1997) Tritiated chiral alkanes as substrates for soluble
methane monooxygenase from Methylococcus capsulatus (Bath): probes for the mechanism
of hydroxylation. J Am Chem Soc 119:1818–1827
40. Ruzicka F, Huang DS, Donnelly MI, Frey PA (1990) Methane monooxygenase catalyzed oxygenation of 1,1-dimethylcyclopropane. Evidence for radical and carbocationic intermediates.
Biochemistry 29:1696–1700
41. Choi SY, Eaton PE, Hollenberg PF, Liu KE, Lippard SJ, Newcomb M, Putt DA, Upadhyaya
SP, Xiong Y (1996) Regiochemical variations in reactions of methylcubane with tert-butoxyl
radical, cytochrome P-450 enzymes, and a methane monooxygenase system. J Am Chem Soc
118:6547–6555
42. Liu KE, Johnson CC, Newcomb M, Lippard SJ (1993) Radical clock substrate probes
and kinetic isotope effect studies of the hydroxylation of hydrocarbons by methane
monooxygenase. J Am Chem Soc 115:939–947
43. Valentine AM, LeTadic-Biadatti MH, 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 274:10771–10776
44. Wilkins PC, Dalton H, Samuel CJ, Green J (1994) Further evidence for multiple pathways in
soluble methane-monooxygenase-catalysed oxidations from the measurement of deuterium
kinetic isotope effects. Eur J Biochem 226:555–560
45. Stahl SS, Francisco WA, Merkx M, Klinman JP, Lippard SJ (2001) Oxygen kinetic isotope
effects in soluble methane monooxygenase. J Biol Chem 276:4549–4553
46. 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 48:12145–12158
47. Yoshizawa K, Yumura T (2003) A non-radical mechanism for methane hydroxylation at the
diiron active site of soluble methane monooxygenase. Chemistry 9:2347–2358
48. Mai BK, Kim Y (2014) Substrate-dependent H/D kinetic isotope effects and the role of the
di(μ-oxo)diiron(IV) core in soluble methane monooxygenase: a theoretical study. Chemistry
20:6532–6541
49. 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
50. Xue G, Pokutsa A, Que L Jr (2011) Substrate-triggered activation of a synthetic [Fe 2 (μ-O) 2 ]
diamond core for C-H bond cleavage. J Am Chem Soc 133:16657–16667
51. Saito T, Shoji M, Isobe H, Yamanaka S, Kitagawa Y, Yamada S, Kawakami T, Okumura M,
Yamaguchi K (2010) Theory of chemical bonds in metalloenzymes. XIV. Correspondence
between magnetic coupling mode and radical coupling mechanism in hydroxylations with
methane monooxygenase and related species. Int J Quant Chem 110:2955–2981
52. Tinberg CE, Lippard SJ (2011) Dioxygen activation in soluble methane monooxygenase. Acc
Chem Res 44:280–288
53. Banerjee R, Jones JC, Lipscomb JD (2019) Soluble methane monooxygenase. Annu Rev
Biochem 88:409–431
54. 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 40:3476–3482
55. 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
123:1794–1795
56. 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 127:5814–5825
57. McCormick MS, Lippard SJ (2011) Analysis of substrate access to active sites in bacterial
multicomponent monooxygenase hydroxylases: X-ray crystal structure of xenon-pressurized
phenol hydroxylase from Pseudomonas sp. OX1. Biochemistry 50:11058–11069