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Journal Article

H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum

MPS-Authors

Schwörer,  Beatrix
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

Zirngibl,  Carmen
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Thauer,  Rudolf K.       
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

External Resource

https://doi.org/10.1111/j.1432-1033.1993.tb17657.x
(Publisher version)

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Citation

Schwörer, B., Fernandez, V. M., Zirngibl, C., & Thauer, R. K. (1993). H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum. European Journal of Biochemistry, 212(1), 255-261. doi:10.1111/j.1432-1033.1993.tb17657.x.


Cite as: https://hdl.handle.net/21.11116/0000-000F-9148-C
Abstract
H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase is a novel hydrogenase found in most methanogenic archaea. It catalyzes the reversible conversion of N5,N10-methylenetetrahydromethanopterin (CH2= H4MPT) to N5,N10-methenyltetrahydromethanopterin (CH ≡ H4MPT+) and dihydrogen; CH2= H4MPT + H+? CH ≡ H4MPT++ H2; ?G°?=+ 5.5 kJ/mol. In the following investigation, the formation of H2, HD and D2 was studied in experiments in which either the methylene group of CH2= H4MPT or water were deuterium labelled. In the case of CD2= H4MPT and H2O, the dihydrogen formed immediately after the start of the reaction was composed of approximately 50% HD and 50% of H2 at all pH tested. In the case of CH2= H4MPT and D2O, the dihydrogen generated was composed of approximately 50% HD and 50% D2 at pD 5.7 and of approximately 85% HD and 15% D2 at pD 7.0. Evidence is presented that the enzyme catalyzes a CH ≡ H4MPT+-dependent isotopic exchange between HD and H2O and between HD and D2O, yielding H2 and D2, respectively. A catalytic mechanism aimed to explain these findings is discussed.