STUDIES OF A “PARTICULATE” FORMIC DEHYDROGENASE FROM ESCHERICHIA COLI

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Abstract
The enzyme system was studied in aerobically-grown cells. Distribution of the enzyme in centrifuged cell-free extracts and inability to fractionate it by classical procedures suggest that the enzyme is associated with bacterial "particles". Trypsin, chymotrypsin or lipase decrease the Tyndall effect exhibited by resuspended "particles" but do not dissolve the "particles". Treatment with lipase and n-butanol yields the enzyme in an apparently soluble form. Soluble formic de-hydrogenase is inhibited by azide, cyanide, p-chloromercuribenzoate, and Cu ions. Enzyme activity is stimulated by Fe2+, Fe3+, and Zn ions. These results indicate that a metal ion and sulfhydryl groups participate in oxidation of formate by this enzyme. The optimum pH for enzyme activity is 6.5.

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