Previous reports suggested that nitrogenase could convert dideuterium (D2) to hydrogen-deuterium (HD) by swapping one hydrogen from water with one deuterium atom. This only happened in the presence of nitrogen. This was tested in various organisms with D2 or D2O as a source of deuterium.
Azotobacter species didn't make HD unless ATP and electrons were present. They actually made less hydrogen and HD with nitrogen than with argon, contradicting earlier findings. 10% CO did inhibit HD formation but not hydrogen formation. Acetylene and methyl isocyanide inhibited HD completely. Cyanide partially or fully inhibited.
There was more exchange with D2O than with D2 for some reason, but this was inhibited more by nitrogen or cyanide.
This seems to have implications for nitrogenase's functions relating to hydrogen.
Reference:
Azotobacter species didn't make HD unless ATP and electrons were present. They actually made less hydrogen and HD with nitrogen than with argon, contradicting earlier findings. 10% CO did inhibit HD formation but not hydrogen formation. Acetylene and methyl isocyanide inhibited HD completely. Cyanide partially or fully inhibited.
There was more exchange with D2O than with D2 for some reason, but this was inhibited more by nitrogen or cyanide.
This seems to have implications for nitrogenase's functions relating to hydrogen.
Reference:
Kelly, M. Hydrogen-deuterium exchange reactions catalysed by nitrogenase. Biochem J 109, 322–324 (1968).
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