Abstract
Previous studies have indicated that nonheme iron may function as an electron carrier in the succinate oxidase pathway of Mycobacterium phlei. The nature and distribution of this component in the bacterium were investigated. A modified method for the quantitative determination of nonheme iron in mammalian and bacterial electron transport systems was developed. The bacterial electron transport particles accounted for only one-fifth of the total protein but were found to contain half of the total iron. In keeping with their electron transport function, the particles contained 89% of the heme iron of the extract. Nonheme iron was released in the ferrous state from particulate and supernatant fractions following boiling with trichloracetic acid. The release of iron from the particulate protein was found to be inhibited by mercurials. This inhibitory action of mercurials was reversed by mercaptoethanol or cysteine. In contrast, mercurials did not inhibit the release of iron from the supernatant protein, but the iron was released in the ferric state. A relation between sulfhydryl groups and iron content was indicated by the action of mercurials. The labile sulfide and flavin adenine dinucleotide content of the bacterial preparations was lower than the content of nonheme iron.
Published Version
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