Abstract
A unidirectional H 2-oxidizing hydrogenase (H 2ase-HO) has been isolated from the anaerobic N 2-fixer Clostridium pasteurianum W5. Extensively purified (> 200-fold or > 400–800 μmoles H 2 oxidized/min/mg protein) H 2ase-HO can use ferredoxin (Fd), methyl viologen (MV), benzyl viologen, methylene blue or dichlorophenolindophenol as the sole electron acceptor but does not produce H 2 from reduced Fd or MV. H 2ase-HO has a lower mol. wt., is less negatively charged and less O 2-sensitive than the classical bidirectional H 2ase from the same organism. The level of the H 2-oxidizing enzyme is higher in N 2-fixing cells than in NH 3-grown cells. H 2ase-HO occurs mainly outside the cell membrane and is inhibited by carbon monoxide.
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More From: Biochemical and Biophysical Research Communications
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