Information from e.p.r. spectroscopy on the iron-sulphur centres of the iron-molybdenum protein (aldehyde oxidoreductase) of Desulfovibrio gigas.
E.p.r. spectra of reduced iron-sulphur centres of the aldehyde oxidoreductase (iron-molybdenum protein) of Desulfovibrio gigas were recorded at X-band and Q-band frequencies and simulated. Results are consistent with the view that only two types of [2Fe-2S] clusters are present, as in eukaryotic molybdenum-containing hydroxylases. The data indicate the Fe/SI centre to be very similar, and the Fe/SII centre somewhat similar, to these centres in the eukaryotic enzymes.
Bray
R C
RC
School of Biological Sciences, University of Sussex, Brighton, U.K.
Turner
N A
NA
Le Gall
J
J
Barata
B A
BA
Moura
J J
JJ
D000445:Aldehyde Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D003901:Desulfovibrio / Q000201:enzymology*; D004578:Electron Spin Resonance Spectroscopy; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008983:Molybdoferredoxin / Q000737:chemistry*
D007506:Iron-Sulfur Proteins; D008983:Molybdoferredoxin; D000445:Aldehyde Oxidoreductases