This study is concerned with the nature of the relatively unusual bonding which occurs in organolithium compounds as a direct result of the oligomerization and possible explanations for that bonding.

The study herein described involved the detection of pyridine N-oxide reductase activity in cell-free extracts of E. coli 9723, the determination of co-factors necessary for the enzymatic process, a study of the optimum conditions for enzyme catalysis, and a general characterization of the enzyme.

The study reported herein concerns itself with the isolation of melaninless mutants of S. antibioticus, ATCC, 3723, and with the demonstration that at least one of the sites of mutation involves that of the enzyme, tyrosinase.

In many series of compounds, intensity of biological activity and chemical reactivity are proportional. Generally whenever a alkyl group replaces a reactive hydrogen atom, as would be the case for an N-substituted hydroxylamine as compared to hydroxylamine, the over-all biological activity of the resulting compound is lower than that of its nonalkylated analogue. Since toxicity and physiological activity are not proportional, this comparison can only suggest possible types of derivatives to prepare and test.