References
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98. Balasubramanian R, Smith SM, Rawat S, Yatsunyk LA, Stemmler TL, Rosenzweig AC (2010)
Oxidation of methane by a biological dicopper centre. Nature 465:115–119
99. Yoshizawa K, Shiota Y (2006) Conversion of methane to methanol at the mononuclear and
dinuclear copper sites of particulate methane monooxygenase (pMMO): a DFT and QM/MM
study. J Am Chem Soc 128:9873–9881
100. Shiota Y, Yoshizawa K (2009) Comparison of the reactivity of bis(μ-oxo)Cu(II)Cu(III) and
Cu(III)Cu(III) species to methane. Inorg Chem 48:838–845
101. Da Silva JC, Pennifold RC, Harvey JN, Rocha WR (2015) A radical rebound mechanism
for the methane oxidation reaction promoted by the dicopper center of a pMMO enzyme: a
computational perspective. Dalton Trans 45:2492–2504
102. Wilkinson B, Zhu M, Priestley ND, Nguyen HHT, Morimoto H, Williams PG, Chan SI, Floss
HG (1996) A concerted mechanism for ethane hydroxylation by the particulate methane
monooxygenase from Methylococcus capsulatus (Bath). J Am Chem Soc 118:921–922
103. Miyaji A, Miyoshi T, Motokura K, Baba T (2015) Discrimination of the prochiral hydrogens
at the C-2 position of n-alkanes by the methane/ammonia monooxygenase family proteins.
Org Biomol Chem 13:8261–8270
104. Mecozzi S, Rebek J Jr (1998) The 55% solution: a formulation for molecular recognition in
the liquid state. Chem Eur J 4:1016–1022
105. Miyaji A, Miyoshi T, Motokura K, Baba T (2011) The substrate binding cavity of particulate methane monooxygenase from Methylosinus trichosporium OB3b expresses high
enantioselectivity for n-butane and n-pentane oxidation to 2-alcohol. Biotechnol Lett
33:2241–2246
106. Park S, Morley K, Horsman GP, Holmquist M, Hult K, Kazlauskas RJ (2005) Focusing mutations into the P. fluorescens esterase binding site increases enantioselectivity more effectively
than distant mutations. Chem Biol 12:45–54
107. Shiemke AK, Cook SA, Miley T, Singleton P (1995) Detergent solubilization of membranebound methane monooxygenase requires plastoquinol analogs as electron donors. Arch
Biochem Biophys 321:421–428
108. Smith DD, Dalton H (1989) Solubilisation of methane monooxygenase from Methylococcus
capsulatus (Bath). Eur J Biochem 182:667–671
109. Takeguchi M, Miyakawa K, Okura I (1998) Properties of the membranes containing the
particulate methane monooxygenase from Methylosinus trichosporium OB3b. Biometals
11:229–234
110. Miyaji A, Nitta M, Baba T (2019) Influence of copper ions removal from membrane-bound
form of particulate methane monooxygenase from Methylosinus trichosporium OB3b on its
activity for methane hydroxylation. J Biotechnol X 1:100001
111. Ribbons DW (1975) Oxidation of C1 compounds by particulate fractions from Methylococcus
capsulatus: distribution and properties of methane-dependent reduced nicotinamide adenine
dinucleotide oxidase (methane hydroxylase). J Bacteriol 122:1351–1363
112. Shiemke AK, Arp DJ, Sayavedra-Soto LA (2004) Inhibition of membrane-bound methane
monooxygenase and ammonia monooxygenase by diphenyliodonium: implications for
electron transfer. J Bacteriol 186:928–937
113. Choi DW, Kunz RC, Boyd ES, Semrau JD, Antholine WE, Han JI, Zahn JA, Boyd JM,
de la Mora AM, DiSpirito AA (2003) The membrane-associated methane monooxygenase (pMMO) and pMMO-NADH:quinone oxidoreductase complex from Methylococcus
capsulatus. Bath. J Bacteriol 185:5755–5764
114. Cornish A, MacDonald J, Burrows KJ, King TS, Scott D, Higgins IJ (1985) Succinate as
an in vitro electron donor for the particulate methane mono-oxygenase of Methylosinus
trichosporium OB3b. Biotech Lett 7:319–324
115. Tonge GM, Harrison DE, Knowles CJ, Higgins IJ (1975) Properties and partial purification of
the methane-oxidising enzyme system from Methylosinus trichosporium. FEBS Lett 58:293–
299
116. Leak DJ, Dalton H (1986) Growth yields of methanotrophs. 1. Effect of copper on the
energetics of methane oxidation. Appl Microbiol Biotechnol 23:470–476
51
98. Balasubramanian R, Smith SM, Rawat S, Yatsunyk LA, Stemmler TL, Rosenzweig AC (2010)
Oxidation of methane by a biological dicopper centre. Nature 465:115–119
99. Yoshizawa K, Shiota Y (2006) Conversion of methane to methanol at the mononuclear and
dinuclear copper sites of particulate methane monooxygenase (pMMO): a DFT and QM/MM
study. J Am Chem Soc 128:9873–9881
100. Shiota Y, Yoshizawa K (2009) Comparison of the reactivity of bis(μ-oxo)Cu(II)Cu(III) and
Cu(III)Cu(III) species to methane. Inorg Chem 48:838–845
101. Da Silva JC, Pennifold RC, Harvey JN, Rocha WR (2015) A radical rebound mechanism
for the methane oxidation reaction promoted by the dicopper center of a pMMO enzyme: a
computational perspective. Dalton Trans 45:2492–2504
102. Wilkinson B, Zhu M, Priestley ND, Nguyen HHT, Morimoto H, Williams PG, Chan SI, Floss
HG (1996) A concerted mechanism for ethane hydroxylation by the particulate methane
monooxygenase from Methylococcus capsulatus (Bath). J Am Chem Soc 118:921–922
103. Miyaji A, Miyoshi T, Motokura K, Baba T (2015) Discrimination of the prochiral hydrogens
at the C-2 position of n-alkanes by the methane/ammonia monooxygenase family proteins.
Org Biomol Chem 13:8261–8270
104. Mecozzi S, Rebek J Jr (1998) The 55% solution: a formulation for molecular recognition in
the liquid state. Chem Eur J 4:1016–1022
105. Miyaji A, Miyoshi T, Motokura K, Baba T (2011) The substrate binding cavity of particulate methane monooxygenase from Methylosinus trichosporium OB3b expresses high
enantioselectivity for n-butane and n-pentane oxidation to 2-alcohol. Biotechnol Lett
33:2241–2246
106. Park S, Morley K, Horsman GP, Holmquist M, Hult K, Kazlauskas RJ (2005) Focusing mutations into the P. fluorescens esterase binding site increases enantioselectivity more effectively
than distant mutations. Chem Biol 12:45–54
107. Shiemke AK, Cook SA, Miley T, Singleton P (1995) Detergent solubilization of membranebound methane monooxygenase requires plastoquinol analogs as electron donors. Arch
Biochem Biophys 321:421–428
108. Smith DD, Dalton H (1989) Solubilisation of methane monooxygenase from Methylococcus
capsulatus (Bath). Eur J Biochem 182:667–671
109. Takeguchi M, Miyakawa K, Okura I (1998) Properties of the membranes containing the
particulate methane monooxygenase from Methylosinus trichosporium OB3b. Biometals
11:229–234
110. Miyaji A, Nitta M, Baba T (2019) Influence of copper ions removal from membrane-bound
form of particulate methane monooxygenase from Methylosinus trichosporium OB3b on its
activity for methane hydroxylation. J Biotechnol X 1:100001
111. Ribbons DW (1975) Oxidation of C1 compounds by particulate fractions from Methylococcus
capsulatus: distribution and properties of methane-dependent reduced nicotinamide adenine
dinucleotide oxidase (methane hydroxylase). J Bacteriol 122:1351–1363
112. Shiemke AK, Arp DJ, Sayavedra-Soto LA (2004) Inhibition of membrane-bound methane
monooxygenase and ammonia monooxygenase by diphenyliodonium: implications for
electron transfer. J Bacteriol 186:928–937
113. Choi DW, Kunz RC, Boyd ES, Semrau JD, Antholine WE, Han JI, Zahn JA, Boyd JM,
de la Mora AM, DiSpirito AA (2003) The membrane-associated methane monooxygenase (pMMO) and pMMO-NADH:quinone oxidoreductase complex from Methylococcus
capsulatus. Bath. J Bacteriol 185:5755–5764
114. Cornish A, MacDonald J, Burrows KJ, King TS, Scott D, Higgins IJ (1985) Succinate as
an in vitro electron donor for the particulate methane mono-oxygenase of Methylosinus
trichosporium OB3b. Biotech Lett 7:319–324
115. Tonge GM, Harrison DE, Knowles CJ, Higgins IJ (1975) Properties and partial purification of
the methane-oxidising enzyme system from Methylosinus trichosporium. FEBS Lett 58:293–
299
116. Leak DJ, Dalton H (1986) Growth yields of methanotrophs. 1. Effect of copper on the
energetics of methane oxidation. Appl Microbiol Biotechnol 23:470–476