Aldehyde oxidoreductase (AOR) activity has been found in different sulfate reducing organisms. The enzyme was purified to homogeneity from extracts of Desulfovibrio desulfuricans (Dd) ATCC 27774, a sulfate reducer that can use sulfate or nitrate as terminal respiratory substrates. The protein (AORDd) is described as a homodimer (monomer, circa 100 kDa), contains a Mo-MCD pterin, 2 x [2Fe-2S] clusters, and lacks a flavin group. Visible and EPR spectroscopies indicate a close similarity with the AOR purified from Desulfovibrio gigas (Dg). Activity and substrate specificity for different aldehydes were determined. EPR studies were performed in native and reduced states of the enzyme and after treatment with ethylene glycol and dithiothreitol. The AORDd was crystallized using ammonium sulfate as precipitant and the crystals belong to the space group P6122, with unit cell dimensions a = b = 156.4 and c = 177.1 Å. These crystals diffract to beyond 2.5 Å resolution and a full data set was measured on a rotating anode generator. The data were used to solve the structure by Patterson Search methods, using the model of AORDg. (C) 2000 Academic Press.
|Number of pages||5|
|Journal||Biochemical And Biophysical Research Communications|
|Publication status||Published - 24 Feb 2000|
- Molybdopterin containing enzymes