46
2 Selective Production of Methanol …
References
1. Hanson RS, Hanson TE (1996) Methanotrophic bacteria. Microbiol Rev 60:439–471
2. Dalton H (2005) The Leeuwenhoek Lecture 2000 The natural and unnatural history of
methane-oxidizing bacteria. Philos Trans R Soc Lond B Biol Sci 360:1207–1222
3. Enger BC, Lødeng R, Holmen A (2008) A review of catalytic partial oxidation of methane
to synthesis gas with emphasis on reaction mechanisms over transition metal catalysts. Appl
Catal A 346:1–27
4. Cruickshank FR, Benson SW (1969) Carbon-hydrogen bond dissociation energy in methanol.
J Phys Chem 733:733–737
5. Nguyen HH, Elliott SJ, Yip JH, Chan SI (1998) The particulate methane monooxygenase
from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme.
Isolation and characterization. J Biol Chem 273:7957–7966
6. Lieberman RL, Rosenzweig AC (2004) Biological methane oxidation: regulation, biochemistry, and active site structure of particulate methane monooxygenase. Crit Rev Biochem Mol
Biol 39:147–164
7. Miyaji A (2011) Particulate methane monooxygenase from Methylosinus trichosporium
OB3b. Methods Enzymol 495:211–225
8. Colby J, Dalton H (1978) Resolution of the methane monooxygenase of Methylococcus
capsulatus (Bath) into three components. Biochem J 171:461–468
9. 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 264:10023–10033
10. Rosenzweig AC, Frederick CA, Lippard SJ, Nordlund P (1993) Crystal structure of a bacterial non-heme iron hydroxylase that catalyzes the biological oxidation of methane. Nature
366:537–543
11. Colby J, Dalton H (1979) Characterization of the second prosthetic group of the flavoenzyme NADH-acceptor reductase (component C) of the methane mono-oxygenase from
Methylococcus capsulatus (Bath). Biochem J 177:903–908
12. 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–
15801
13. 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 2:409–418
14. Rosenzweig AC, Brandstetter H, Whittington DA, Nordlund P, Lippard SJ, Frederick CA
(1997) Crystal structure of the methane monooxygenase hydroxylase from Methylococcus
capsulatus (Bath): implications for substrate gating and component interactions. Proteins
29:141–152
15. Whittington DA, Lippard SJ (2001) Crystal structures of the soluble methane monooxygenase
hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometric variability at
the dinuclear iron active site. J Am Chem Soc 123:827–838
16. Elango N, Radhakrishnan R, Froland WA, Wallar BJ, Earhart CA, Lipscomb JD, Ohlendorf
DH (1997) Crystal structure of the hydroxylase component of methane monooxygenase from
Methylosinus trichosporium OB3b. Protein Sci 6:556–568
17. Pulver SC, Froland WA, Fox BG, Lipscomb JD, Solomon EI (1993) Spectroscopic studies of
the coupled binuclear non-heme iron active site in the fully reduced hydroxylase component
of methane monooxygenase: comparison to deoxy and deoxyazide hemerythrin. J Am Chem
Soc 115:12409–12422
18. Pulver SC, Froland WA, Lipscomb JD, Solomon EI (1997) Ligand field circular dichroism and
magnetic circular dichroism studies of component B and substrate binding to the hydroxylase
component of methane monooxygenase. J Am Chem Soc 119:387–395
19. Lee SK, Nesheim JC, Lipscomb JD (1993) Transient intermediates of the methane monooxygenase catalytic cycle. J Biol Chem 268:21569–21577
2 Selective Production of Methanol …
References
1. Hanson RS, Hanson TE (1996) Methanotrophic bacteria. Microbiol Rev 60:439–471
2. Dalton H (2005) The Leeuwenhoek Lecture 2000 The natural and unnatural history of
methane-oxidizing bacteria. Philos Trans R Soc Lond B Biol Sci 360:1207–1222
3. Enger BC, Lødeng R, Holmen A (2008) A review of catalytic partial oxidation of methane
to synthesis gas with emphasis on reaction mechanisms over transition metal catalysts. Appl
Catal A 346:1–27
4. Cruickshank FR, Benson SW (1969) Carbon-hydrogen bond dissociation energy in methanol.
J Phys Chem 733:733–737
5. Nguyen HH, Elliott SJ, Yip JH, Chan SI (1998) The particulate methane monooxygenase
from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme.
Isolation and characterization. J Biol Chem 273:7957–7966
6. Lieberman RL, Rosenzweig AC (2004) Biological methane oxidation: regulation, biochemistry, and active site structure of particulate methane monooxygenase. Crit Rev Biochem Mol
Biol 39:147–164
7. Miyaji A (2011) Particulate methane monooxygenase from Methylosinus trichosporium
OB3b. Methods Enzymol 495:211–225
8. Colby J, Dalton H (1978) Resolution of the methane monooxygenase of Methylococcus
capsulatus (Bath) into three components. Biochem J 171:461–468
9. 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 264:10023–10033
10. Rosenzweig AC, Frederick CA, Lippard SJ, Nordlund P (1993) Crystal structure of a bacterial non-heme iron hydroxylase that catalyzes the biological oxidation of methane. Nature
366:537–543
11. Colby J, Dalton H (1979) Characterization of the second prosthetic group of the flavoenzyme NADH-acceptor reductase (component C) of the methane mono-oxygenase from
Methylococcus capsulatus (Bath). Biochem J 177:903–908
12. 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–
15801
13. 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 2:409–418
14. Rosenzweig AC, Brandstetter H, Whittington DA, Nordlund P, Lippard SJ, Frederick CA
(1997) Crystal structure of the methane monooxygenase hydroxylase from Methylococcus
capsulatus (Bath): implications for substrate gating and component interactions. Proteins
29:141–152
15. Whittington DA, Lippard SJ (2001) Crystal structures of the soluble methane monooxygenase
hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometric variability at
the dinuclear iron active site. J Am Chem Soc 123:827–838
16. Elango N, Radhakrishnan R, Froland WA, Wallar BJ, Earhart CA, Lipscomb JD, Ohlendorf
DH (1997) Crystal structure of the hydroxylase component of methane monooxygenase from
Methylosinus trichosporium OB3b. Protein Sci 6:556–568
17. Pulver SC, Froland WA, Fox BG, Lipscomb JD, Solomon EI (1993) Spectroscopic studies of
the coupled binuclear non-heme iron active site in the fully reduced hydroxylase component
of methane monooxygenase: comparison to deoxy and deoxyazide hemerythrin. J Am Chem
Soc 115:12409–12422
18. Pulver SC, Froland WA, Lipscomb JD, Solomon EI (1997) Ligand field circular dichroism and
magnetic circular dichroism studies of component B and substrate binding to the hydroxylase
component of methane monooxygenase. J Am Chem Soc 119:387–395
19. Lee SK, Nesheim JC, Lipscomb JD (1993) Transient intermediates of the methane monooxygenase catalytic cycle. J Biol Chem 268:21569–21577