Properties of the tungsten-substituted molybdenum formylmethanofuran dehydrogenase from Methanobacterium wolfei.
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.
Schmitz
R A
RA
Laboratorium für Mikrobiologie, Fachbereichs Biologie, Phillipps-Universität, Marburg, Germany.
Albracht
S P
SP
Thauer
R K
RK
D000445:Aldehyde Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D003198:Computer Simulation; D004578:Electron Spin Resonance Spectroscopy; D007700:Kinetics; D017014:Methanobacterium / Q000201:enzymology*; D008970:Molecular Weight; D008982:Molybdenum / Q000032:analysis / Q000378:metabolism*; D014414:Tungsten / Q000494:pharmacology*
D008982:Molybdenum; D000445:Aldehyde Oxidoreductases; C060639:formylmethanofuran dehydrogenase; D014414:Tungsten