The concentration-dependence of the inhibition of whole-cell hydrogen formation by oxygen has been measured in the trichomonads and compared with the oxygen inhibition of the hydrogenase activity as measured by a tritium exchange assay. The inhibition profiles closely paralleled each other, suggesting that hydrogenase is the primary site of inhibition of anaerobic fermentative metabolism. In addition the inhibition profile for isolated hydrogenosomes was measured and shown to be similar to that for whole organisms. Ascorbate peroxidase was shown to be present in both organisms whereas catalase was confirmed to be present only in The kinetic parameters of both enzymes were measured and their respective roles in oxygen protection discussed.


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