Molybdenum and vanadium nitrogenases of Azotobacter chroococcum. Low temperature favours N2 reduction by vanadium nitrogenase.
A comparison of the effect of temperature on the reduction of N2 by purified molybdenum nitrogenase and vanadium nitrogenase of Azotobacter chroococcum showed differences in behaviour. As the assay temperature was lowered from 30 degrees C to 5 degrees C N2 remained an effective substrate for V nitrogenase, but not Mo nitrogenase, since the specific activity for N2 reduction by Mo nitrogenase decreased 10-fold more than that of V nitrogenase. Activity cross-reactions between nitrogenase components showed the enhanced low-temperature activity to be associated with the Fe protein of V nitrogenase. The lower activity of homologous Mo nitrogenase components, although dependent on the ratio of MoFe protein to Fe protein, did not equal that of V nitrogenase even under conditions of high electron flux obtained at a 12-fold molar excess of Fe protein.
Miller
R W
RW
Plant Research Centre, Agriculture Canada, Ottawa, Ontario.
Eady
R R
RR
D001395:Azotobacter / Q000201:enzymology*; D001426:Bacterial Proteins; D008667:Metalloproteins / Q000378:metabolism; D008982:Molybdenum / Q000378:metabolism*; D009584:Nitrogen / Q000378:metabolism*; D009591:Nitrogenase / Q000378:metabolism*; D010084:Oxidation-Reduction; D013696:Temperature; D014639:Vanadium / Q000378:metabolism*
D001426:Bacterial Proteins; D008667:Metalloproteins; C052750:vanadium-iron protein, Azotobacter; D014639:Vanadium; D008982:Molybdenum; D009591:Nitrogenase; D009584:Nitrogen