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Properties of the tungsten-substituted molybdenum formylmethanofuran dehydrogenase from Methanobacterium wolfei

MPS-Authors

Schmitz,  R.A.
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,  R. K.       
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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Citation

Schmitz, R., Albracht, S., & Thauer, R. K. (1992). Properties of the tungsten-substituted molybdenum formylmethanofuran dehydrogenase from Methanobacterium wolfei. FEBS Letters, 309(1), 78-81. doi:10.1016/0014-5793(92)80743-Z.


Cite as: https://hdl.handle.net/21.11116/0000-000F-911F-B
Abstract
In Methanobacterium wolfei two formylmethanofuran dehydrogenases are present, one of which is a molybdenum- and the other a tungsten enzyme. We report here that also the ‘molybdenum’ enzyme contained tungsten when the archaeon was grown on molybdenum-deprived medium supplemented with tungstate (1 μM). Unexpectedly the tungsten-substituted molybdenum enzyme was catalytically active and displayed a rhombic EPR signal which was attributed to tungsten by the characteristic 113W splitting.