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Journal Article

Si-face stereospecificity at C5 of coenzyme F420 for F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase, F420-dependent N5,N10-methylenetetrahydromethanopterin reductase and F420H2:dimethylnaphthoquinone oxidoreductase

MPS-Authors

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

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

Setzke,  Edgar
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.tb17964.x
(Publisher version)

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Citation

Kunow, J., Schwörer, B., Setzke, E., & Thauer, R. K. (1993). Si-face stereospecificity at C5 of coenzyme F420 for F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase, F420-dependent N5,N10-methylenetetrahydromethanopterin reductase and F420H2:dimethylnaphthoquinone oxidoreductase. European Journal of Biochemistry, 214(3), 641-646. doi:10.1111/j.1432-1033.1993.tb17964.x.


Cite as: https://hdl.handle.net/21.11116/0000-000F-91D5-C
Abstract
Coenzyme F420-dependent enzymes catalyze the reversible reduction of F420 by stereospecific hydride transfer to C5 of 5-deazaflavin. Two F420-dependent enzymes have been investigated with respect to the stereochemistry of hydride transfer, the F420-dependent NADP reductase and the F420-reducing hydrogenase. Both enzymes were found to be Si-face specific. In this study we report that three additional F420-dependent enzymes are also Si-face specific: N5,N10-methylenetetrahydromethanopterin dehydrogenase, N5,N10-methylenetetrahydromethanopterin reductase and coenzyme F420H2: dimethylnaphthoquinone oxidoreductase (F420H2 dehydrogenase). Thus, all five characterized F420-dependent enzymes are Si-face specific, which is noteworthy since coenzyme F420 is functionally similar to pyridine nucleotides and both Si-face specific and Re-face specific pyridine-nucleotide-dependent enzymes exist.