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Properties of the tungsten-substituted molybdenum formylmethanofuran dehydrogenase from Methanobacterium wolfei
R A Schmitz1, S P Albracht, R K Thauer
1Laboratorium für Mikrobiologie, Fachbereichs Biologie, Phillipps-Universität, Marburg, Germany.
FEBS Letters
|August 31, 1992
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 microM). Unexpectedly the tungsten-substituted molybdenum enzyme was catalytically active and displayed a rhombic EPR signal which was attributed to tungsten by the characteristic 183W splitting.