PROPERTIES OF HYDROGENASE FROM AZOTOBACTER VINELANDII

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Abstract
Hydrogenase in cell-free juices of A. vinelandii was associated largely with small particles. The enzyme was stable and was not affected by addition of co-factors. The absorption spectrum suggested the presence of a hemoprotein component. Hydrogenase was inhibited by CO, but the inhibition was not light-reversible. The exchange reaction between H2 and D2O was slow. Crude juices carried out the Knallgas reaction with esterification of phosphate via adenosine-5-phosphoric acid.