Characterization of the chlorate reductase from Pseudomonas chloritidismutans.
A chlorate reductase has been purified from the chlorate-reducing strain Pseudomonas chloritidismutans. Comparison with the periplasmic (per)chlorate reductase of strain GR-1 showed that the cytoplasmic chlorate reductase of P. chloritidismutans reduced only chlorate and bromate. Differences were also found in N-terminal sequences, molecular weight, and subunit composition. Metal analysis and electron paramagnetic resonance measurements showed the presence of iron and molybdenum, which are also found in other dissimilatory oxyanion reductases.
Wolterink
Arthur F W M
AF
Laboratory of Microbiology, Wageningen University, 6703 CT Wageningen, The Netherlands.
Schiltz
Emile
E
Hagedoorn
Peter-Leon
PL
Hagen
Wilfred R
WR
Kengen
Servé W M
SW
Stams
Alfons J M
AJ
D000595:Amino Acid Sequence; D003593:Cytoplasm / Q000201:enzymology; D004578:Electron Spin Resonance Spectroscopy; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008982:Molybdenum / Q000378:metabolism; D010088:Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology*; D020539:Sequence Analysis, Protein; D013696:Temperature
D008982:Molybdenum; D010088:Oxidoreductases; C021777:chlorate reductase