References
47
20. Lee SK, Fox BG, Froland WA, Lipscomb JD, Münck E (1993) A transient intermediate of
the methane monooxygenase catalytic cycle containing an Fe(IV)-Fe(IV) cluster. J Am Chem
Soc 115:6450–6451
21. Lee SY, Lipscomb JD (1999) Oxygen activation catalyzed by methane monooxygenase
hydroxylase component: proton delivery during the O-O bond cleavage steps. Biochemistry
38:4423–4432
22. Liu KE, Valentine AM, Wang DL, Huynh BH, Edmondson DE, Salifoglou A, Lippard SJ
(1995) Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methylococcus capsulatus (Bath). J Am
Chem Soc 117:10174–10185
23. Shu LJ, Nesheim JC, Kauffmann K, Münck E, Lipscomb JD, Que L Jr (1997) An Fe(IV)O 2 diamond core structure for the key intermediate Q of methane monooxygenase. Science
275:515–518
24. Brazeau BJ, Lipscomb JD (2000) Kinetics and activation thermodynamics of methane
monooxygenase hydroxylase compound Q formation and reaction with substrates. Biochemistry 39:13503–13515
25. DeWitt JG, Bentsen JG, Rosenzweig AC, Hedman B, Green J, Pilkington S, Papaefthymiou
GC, Dalton H, Hodgson KO, Lippard SJ (1991) X-ray absorption, Moessbauer, and EPR
studies of the dinuclear iron center in the hydroxylase component of methane monooxygenase.
J Am Chem Soc 113:9219–9235
26. Woodland MP, Patil DS, Cammack R, Dalton H (1986) ESR studies of protein A of the
soluble methane monooxygenase from Methylococcus capsulatus (Bath). Biochim Biophys
Acta 873:237–242
27. Ericson A, Hedman B, Hodgson KO, Green J, Dalton H, Bentsen JG, Beer RH, Lippard SJ
(1988) J Am Chem Soc 110:2330–2332
28. Banerjee R, Proshlyakov Y, Lipscomb JD, Proshlyakov DA (2015) Structure of the key species
in the enzymatic oxidation of methane to methanol. Nature 518:431–434
29. Rinaldo D, Philipp DM, Lippard SJ, Friesner RAJ (2007) Intermediates in dioxygen activation
by methane monooxygenase: a QM/MM study. J Am Chem Soc 129:3135–3147
30. Han WG, Noodleman L (2008) Structural model studies for the high-valent intermediate Q of
methane monooxygenase from broken-symmetry density functional calculations. Inorg Chim
Acta 361:973–986
31. Siegbahn PEM, Crabtree RH, Nordlund P (1998) Mechanism of methane monooxygenase—a
structural and quantum chemical perspective. J Biol Inorg Chem 3:314–317
32. Siegbahn PEM (1999) Theoretical model studies of the iron dimer complex of MMO and
RNR. Inorg Chem 38:2880–2889
33. Lovell T, Han WG, Liu TQ, Noodleman L (2002) A structural model for the high-valent
intermediate Q of methane monooxygenase from broken-symmetry density functional and
electrostatics calculations. J Am Chem Soc 124:5890–5894
34. Friedle S, Reisner E, Lippard S (2010) Current challenges of modeling diiron enzyme active
sites for dioxygen activation by biomimetic synthetic complexes. J Chem Soc Rev 39:2768–
2779
35. Huang SP, Shiota Y, Yoshizawa K (2013) DFT study of the mechanism for methane hydroxylation by soluble methane monooxygenase (sMMO): effects of oxidation state, spin state,
and coordination number. Dalton Trans 42:1011–1023
36. Xue G, Wang D, De Hont R, Fiedler AT, Shan X, Münck E, Que L Jr (2007) A synthetic precedent for the Fe IV
2 (μ − O) 2 ] diamond core proposed for methane monooxygenase intermediate
Q. Proc Natl Acad Sci USA 104:20713–20718
37. Cutsail GE 3rd, Banerjee R, Zhou A, Que L Jr, 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 140:16807–16820
38. Priestley ND, Floss HG, Froland WA, Lipscomb JD, Williams PG, Morimoto H (1992) Cryptic
stereospecificity of methane monooxygenase. J Am Chem Soc 114:7561–7562
47
20. Lee SK, Fox BG, Froland WA, Lipscomb JD, Münck E (1993) A transient intermediate of
the methane monooxygenase catalytic cycle containing an Fe(IV)-Fe(IV) cluster. J Am Chem
Soc 115:6450–6451
21. Lee SY, Lipscomb JD (1999) Oxygen activation catalyzed by methane monooxygenase
hydroxylase component: proton delivery during the O-O bond cleavage steps. Biochemistry
38:4423–4432
22. Liu KE, Valentine AM, Wang DL, Huynh BH, Edmondson DE, Salifoglou A, Lippard SJ
(1995) Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methylococcus capsulatus (Bath). J Am
Chem Soc 117:10174–10185
23. Shu LJ, Nesheim JC, Kauffmann K, Münck E, Lipscomb JD, Que L Jr (1997) An Fe(IV)O 2 diamond core structure for the key intermediate Q of methane monooxygenase. Science
275:515–518
24. Brazeau BJ, Lipscomb JD (2000) Kinetics and activation thermodynamics of methane
monooxygenase hydroxylase compound Q formation and reaction with substrates. Biochemistry 39:13503–13515
25. DeWitt JG, Bentsen JG, Rosenzweig AC, Hedman B, Green J, Pilkington S, Papaefthymiou
GC, Dalton H, Hodgson KO, Lippard SJ (1991) X-ray absorption, Moessbauer, and EPR
studies of the dinuclear iron center in the hydroxylase component of methane monooxygenase.
J Am Chem Soc 113:9219–9235
26. Woodland MP, Patil DS, Cammack R, Dalton H (1986) ESR studies of protein A of the
soluble methane monooxygenase from Methylococcus capsulatus (Bath). Biochim Biophys
Acta 873:237–242
27. Ericson A, Hedman B, Hodgson KO, Green J, Dalton H, Bentsen JG, Beer RH, Lippard SJ
(1988) J Am Chem Soc 110:2330–2332
28. Banerjee R, Proshlyakov Y, Lipscomb JD, Proshlyakov DA (2015) Structure of the key species
in the enzymatic oxidation of methane to methanol. Nature 518:431–434
29. Rinaldo D, Philipp DM, Lippard SJ, Friesner RAJ (2007) Intermediates in dioxygen activation
by methane monooxygenase: a QM/MM study. J Am Chem Soc 129:3135–3147
30. Han WG, Noodleman L (2008) Structural model studies for the high-valent intermediate Q of
methane monooxygenase from broken-symmetry density functional calculations. Inorg Chim
Acta 361:973–986
31. Siegbahn PEM, Crabtree RH, Nordlund P (1998) Mechanism of methane monooxygenase—a
structural and quantum chemical perspective. J Biol Inorg Chem 3:314–317
32. Siegbahn PEM (1999) Theoretical model studies of the iron dimer complex of MMO and
RNR. Inorg Chem 38:2880–2889
33. Lovell T, Han WG, Liu TQ, Noodleman L (2002) A structural model for the high-valent
intermediate Q of methane monooxygenase from broken-symmetry density functional and
electrostatics calculations. J Am Chem Soc 124:5890–5894
34. Friedle S, Reisner E, Lippard S (2010) Current challenges of modeling diiron enzyme active
sites for dioxygen activation by biomimetic synthetic complexes. J Chem Soc Rev 39:2768–
2779
35. Huang SP, Shiota Y, Yoshizawa K (2013) DFT study of the mechanism for methane hydroxylation by soluble methane monooxygenase (sMMO): effects of oxidation state, spin state,
and coordination number. Dalton Trans 42:1011–1023
36. Xue G, Wang D, De Hont R, Fiedler AT, Shan X, Münck E, Que L Jr (2007) A synthetic precedent for the Fe IV
2 (μ − O) 2 ] diamond core proposed for methane monooxygenase intermediate
Q. Proc Natl Acad Sci USA 104:20713–20718
37. Cutsail GE 3rd, Banerjee R, Zhou A, Que L Jr, 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 140:16807–16820
38. Priestley ND, Floss HG, Froland WA, Lipscomb JD, Williams PG, Morimoto H (1992) Cryptic
stereospecificity of methane monooxygenase. J Am Chem Soc 114:7561–7562