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Properties of Nonheme Iron in a Cell Envelope Fraction from Escherichia coli

Department of Biochemistry, University of British Columbia, Vancouver, B. C., Canada

ABSTRACT

The reaction with o-phenanthroline of nonheme iron found in cell envelope fractions from Escherichia coli has been investigated. About 20% of the total nonheme iron reacts directly with o-phenanthroline. This iron appears to be in the ferric state but is reducible by protein sulfhydryl groups in the presence of the chelating agent. A further 20% of the nonheme iron will react with o-phenanthroline only in the presence of dithionite. Succinate can replace dithionite but only produces about 35% of the reaction given by dithionite. The reduction of cytochrome b₁ of the respiratory chain by succinate shows similar behavior to the reaction of iron with o-phenanthroline in the presence of succinate. Both of these components react completely only in the presence of 2-heptyl-4-hydroxyquinoline-N-oxide. The remaining 60% of the nonheme iron of the cell envelope will not react with o-phenanthroline even in the presence of dithionite or 6 M urea. Triton X-100 with dithionite will permit a small part (10%) of this iron to react with o-phenanthroline. The iron which does not react with o-phenanthroline is not associated with succinate, reduced nicotinamide adenine dinucleotide, or D-lactate dehydrogenases.

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• Zhu, W., Hunt, D. J., Richardson, A. R., Stojiljkovic, I. (2000). Use of Heme Compounds as Iron Sources by Pathogenic Neisseriae Requires the Product of the hemO Gene. J. Bacteriol. 182: 439-447 [Abstract] [Full Text]