Cyanide formation from glyoxylate and hydroxylamine catalysed by extracts of higher-plant leaves.

Extracts of spinach, maize and barley contain an enzyme which catalyses the formation of hydrogen cyanide from glyoxylate and hydroxylamine. The enzyme is dependent upon ADP and a divalent cation such as manganese. Glyoxylicacid oxime is a poor substrate for the enzyme. Carbon dioxide is another product of the reaction and is probably produced in 1:1 stoichiometry with hydrogen cyanide. The possible relationship of this enzyme to the regulation of nitrate reduction is discussed.

Metabolism of hydroxylamine by spinach leaf discs and its relationship to nitrate reduction.

Nitrate reduction in vivo by spinach leaf discs was shown to be inhibited by hydroxylamine when this was included in the nitrate reductase assay solutions or introduced to the tissue during a preincubation period. The sensitivity of nitrate reduction to hydroxylamine was not sufficient to suggest a natural process, considering the small endogenous concentrations of hydroxylamine in the leaves. Inhibition of nitrate reduction in vivo could be approximately related to rates of in vitro inhibition of nitrate reductase by this compound. There was no need to suppose conversion of hydroxylamine to cyanide to inhibit nitrate reduction. Some of the in vivo and in vitro characteristics of hydroxylamine inhibition of nitrate reductase are described. Hydroxylamine was metabolised by discs at rates comparable to nitrate reduction. Rates of metabolism of hydroxylamine, and its accumulation in the tissues from an external solution were both enhanced by light but little affected by anaerobiosis.