How Metal Coordination in the Ca-, Ce- and Eu-Containing …
499
FR (eds) Microbial growth on C1 compounds. Kluwer Academic Publishers, Dordrecht, pp
126–132
7. Hibi Y, Asai K, Arafuka H, Hamajima M, Iwama T, Kawai K (2011) Molecular structure
of La 3+ -induced methanol dehydrogenase-like protein in Methylobacterium radiotolerans. J
Biosci Bioeng 111:547–549. https://doi.org/10.1016/j.jbiosc.2010.12.017
8. Chistoserdova L (2016) Lanthanides: new life metals? World J Microbiol Biotechnol 32:138.
https://doi.org/10.1007/s11274-016-2088-2
9. Anthony C (2000) Methanol dehydrogenase, a PQQ-containing quinoprotein dehydrogenase.
In: Holzenburg A, Scrutton NS (eds) Enzyme-catalyzed electron and radical transfer, vol 35.
Springer, New York
10. Anthony C (2004) The quinoprotein dehydrogenases for methanol and glucose. Arch Biochem
Biophys 428:2–9. https://doi.org/10.1016/j.abb.2004.03.038
11. Goodwin PM, Anthony C (1998) The biochemistry, physiology and genetics of PQQ
and PQQ-containing enzymes. Adv Microb Physiol 40:1–80. https://doi.org/10.1016/S00652911(08)60129-0
12. Cotton S (2006) Lanthanide and actinide chemistry. Wiley, Chichester; Evans CH (1990) Biochemistry of the lanthanides. Springer, New York
13. Shiller AM, Chan EW, Joung DJ, Redmond MC, Kessler JD (2017) Light rare earth element
depletion during Deepwater Horizon blowout methanotrophy. Sci Rep 7:1–9. https://doi.org/
10.1038/s41598-017-11060-z
14. Vu HN, Subuyuj GA, Vijayakumar S, Good NM, Martinez-Gomez NC, Skovran E
(2016) Lanthanide-dependent regulation of methanol oxidation systems in Methylobacterium
extorquensAM1 and their contribution to methanol growth. J Bacteriol 198:1250–1259. https://
doi.org/10.1128/JB.00937-15
15. Ochsner AM, Sonntag F, Buchhaupt M, Schrader J, Vorholt JA (2015) Methylobacterium
extorquens: methylotrophy and biotechnological applications. Appl Microbiol Biotechnol
99:517–534. https://doi.org/10.1007/s00253-014-6240-3
16. Semrau JD, Di Spirito AA, Gu W, Yoon S (2018) Metals and methanotrophy. Appl Environ
Microbiol 84:e02289–17. https://doi.org/10.1128/AEM.02289-17
17. Pol A, Barends TRM, Dietl A, Khadem AF, Eygensteyn J, Jetten MSM, Op den Camp HJM
(2014) Rare earth metals are essential for methanotrophic life in volcanic mudpots. Environ
Microbiol 16:255–264. https://doi.org/10.1111/1462-2920.12249
18. Afolabi PR, Mohammed F, Amaratunga K, Majekodunmi O, Dales L, Gill R, Thompson
D, Cooper B, Wood P, Goodwin M, Anthony C (2001) Site-directed mutagenesis and X-ray
crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron
acceptor, cytochrome cL. Biochemistry 40:9799–9809. https://doi.org/10.1021/bi002932l
19. Jahn B, Pol A, Lumpe H, Barends TRM, Dietl A, Hogendoorn C, Op den Camp HJM, Daumann LJ (2018) Similar but not the same: first kinetic and structural analyses of a methanol
dehydrogenase containing a europium ion in the active site. ChemBioChem 19:1147–1153.
https://doi.org/10.1002/cbic.201800130
20. Zheng YJ, Bruice TC (1997) Conformation of coenzyme pyrroloquinoline quinone and
role of Ca 2+ in the catalytic mechanism of quinoprotein methanol dehydrogenase. PNAS
94:11881–11886. https://doi.org/10.1073/pnas.94.22.11881
21. Zheng YJ, Xia Z, Chen Z, Mathews FS, Bruice TC (2001) Catalytic mechanism of quinoprotein methanol dehydrogenase: a theoretical and X-ray crystallographic investigation. PNAS
98:432–434. https://doi.org/10.1073/pnas.98.2.432
22. Idupulapati NB, Mainardi DS (2010) Quantum chemical modeling of methanol oxidation
mechanisms by methanol dehydrogenase enzyme: effect of substitution of calcium by barium
in the active site. J Phys Chem A 114:1887–1896. https://doi.org/10.1021/jp9083025
23. Leopoldini M, Russo N, Toscano M (2007) The preferred reaction path for the oxidation of
methanol by PQQ-containing methanol dehydrogenase: addition-elimination versus hydridetransfer mechanism. Chem Eur J 13:2109–2117. https://doi.org/10.1002/chem.200601123
24. Hothi P, Sutcliffe MJ, Scrutton NS (2005) Kinetic isotope effects and ligand binding in
PQQ-dependent methanol dehydrogenase. Biochem J 388:123–133. https://doi.org/10.1042/
BJ20041731
499
FR (eds) Microbial growth on C1 compounds. Kluwer Academic Publishers, Dordrecht, pp
126–132
7. Hibi Y, Asai K, Arafuka H, Hamajima M, Iwama T, Kawai K (2011) Molecular structure
of La 3+ -induced methanol dehydrogenase-like protein in Methylobacterium radiotolerans. J
Biosci Bioeng 111:547–549. https://doi.org/10.1016/j.jbiosc.2010.12.017
8. Chistoserdova L (2016) Lanthanides: new life metals? World J Microbiol Biotechnol 32:138.
https://doi.org/10.1007/s11274-016-2088-2
9. Anthony C (2000) Methanol dehydrogenase, a PQQ-containing quinoprotein dehydrogenase.
In: Holzenburg A, Scrutton NS (eds) Enzyme-catalyzed electron and radical transfer, vol 35.
Springer, New York
10. Anthony C (2004) The quinoprotein dehydrogenases for methanol and glucose. Arch Biochem
Biophys 428:2–9. https://doi.org/10.1016/j.abb.2004.03.038
11. Goodwin PM, Anthony C (1998) The biochemistry, physiology and genetics of PQQ
and PQQ-containing enzymes. Adv Microb Physiol 40:1–80. https://doi.org/10.1016/S00652911(08)60129-0
12. Cotton S (2006) Lanthanide and actinide chemistry. Wiley, Chichester; Evans CH (1990) Biochemistry of the lanthanides. Springer, New York
13. Shiller AM, Chan EW, Joung DJ, Redmond MC, Kessler JD (2017) Light rare earth element
depletion during Deepwater Horizon blowout methanotrophy. Sci Rep 7:1–9. https://doi.org/
10.1038/s41598-017-11060-z
14. Vu HN, Subuyuj GA, Vijayakumar S, Good NM, Martinez-Gomez NC, Skovran E
(2016) Lanthanide-dependent regulation of methanol oxidation systems in Methylobacterium
extorquensAM1 and their contribution to methanol growth. J Bacteriol 198:1250–1259. https://
doi.org/10.1128/JB.00937-15
15. Ochsner AM, Sonntag F, Buchhaupt M, Schrader J, Vorholt JA (2015) Methylobacterium
extorquens: methylotrophy and biotechnological applications. Appl Microbiol Biotechnol
99:517–534. https://doi.org/10.1007/s00253-014-6240-3
16. Semrau JD, Di Spirito AA, Gu W, Yoon S (2018) Metals and methanotrophy. Appl Environ
Microbiol 84:e02289–17. https://doi.org/10.1128/AEM.02289-17
17. Pol A, Barends TRM, Dietl A, Khadem AF, Eygensteyn J, Jetten MSM, Op den Camp HJM
(2014) Rare earth metals are essential for methanotrophic life in volcanic mudpots. Environ
Microbiol 16:255–264. https://doi.org/10.1111/1462-2920.12249
18. Afolabi PR, Mohammed F, Amaratunga K, Majekodunmi O, Dales L, Gill R, Thompson
D, Cooper B, Wood P, Goodwin M, Anthony C (2001) Site-directed mutagenesis and X-ray
crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron
acceptor, cytochrome cL. Biochemistry 40:9799–9809. https://doi.org/10.1021/bi002932l
19. Jahn B, Pol A, Lumpe H, Barends TRM, Dietl A, Hogendoorn C, Op den Camp HJM, Daumann LJ (2018) Similar but not the same: first kinetic and structural analyses of a methanol
dehydrogenase containing a europium ion in the active site. ChemBioChem 19:1147–1153.
https://doi.org/10.1002/cbic.201800130
20. Zheng YJ, Bruice TC (1997) Conformation of coenzyme pyrroloquinoline quinone and
role of Ca 2+ in the catalytic mechanism of quinoprotein methanol dehydrogenase. PNAS
94:11881–11886. https://doi.org/10.1073/pnas.94.22.11881
21. Zheng YJ, Xia Z, Chen Z, Mathews FS, Bruice TC (2001) Catalytic mechanism of quinoprotein methanol dehydrogenase: a theoretical and X-ray crystallographic investigation. PNAS
98:432–434. https://doi.org/10.1073/pnas.98.2.432
22. Idupulapati NB, Mainardi DS (2010) Quantum chemical modeling of methanol oxidation
mechanisms by methanol dehydrogenase enzyme: effect of substitution of calcium by barium
in the active site. J Phys Chem A 114:1887–1896. https://doi.org/10.1021/jp9083025
23. Leopoldini M, Russo N, Toscano M (2007) The preferred reaction path for the oxidation of
methanol by PQQ-containing methanol dehydrogenase: addition-elimination versus hydridetransfer mechanism. Chem Eur J 13:2109–2117. https://doi.org/10.1002/chem.200601123
24. Hothi P, Sutcliffe MJ, Scrutton NS (2005) Kinetic isotope effects and ligand binding in
PQQ-dependent methanol dehydrogenase. Biochem J 388:123–133. https://doi.org/10.1042/
BJ20041731