Formylmethanofuran dehydrogenase from methanogenic bacteria, a molybdoenzyme.
Formylmethanofuran dehydrogenase, a key enzyme of methanogenesis, was purified 100-fold from methanol grown Methanosarcina barkeri to apparent homogeneity and a specific activity of 34 mumol.min-1.mg protein-1. Molybdenum was found to co-migrate with the enzyme activity. The molybdenum content of purified preparations was 3-4 nmol per mg protein equal to 0.6-0.8 mol molybdenum per mol enzyme of apparent molecular mass 200 kDa. Evidence is presented that also formylmethanofuran dehydrogenase from H2/CO2 grown Methanobacterium thermoautotrophicum (strain Marburg) is a molybdoenzyme.
Karrasch
M
M
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität, Marburg, FRG.
Börner
G
G
Enssle
M
M
Thauer
R K
RK
D000445:Aldehyde Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D004579:Electron Transport; D019605:Euryarchaeota / Q000201:enzymology*; D005663:Furans / Q000378:metabolism*; D008667:Metalloproteins / Q000378:metabolism*; D008982:Molybdenum / Q000378:metabolism*; D013057:Spectrum Analysis
D005663:Furans; D008667:Metalloproteins; D008982:Molybdenum; C050842:formylmethanofuran; D000445:Aldehyde Oxidoreductases; C060639:formylmethanofuran dehydrogenase