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- W1607148211 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 b 1 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." @default.
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- W1607148211 date "1971-09-01" @default.
- W1607148211 modified "2023-09-23" @default.
- W1607148211 title "Properties of Nonheme Iron in a Cell Envelope Fraction from Escherichia coli" @default.
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- W1607148211 doi "https://doi.org/10.1128/jb.107.3.664-670.1971" @default.
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