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Soluble and membrane-bound ferrisiderophore reductases of Escherichia coli K-12 by Eckhard Fischer; Birgit Strehlow; Dieter Hartz; Volkmar Braun is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Soluble and membrane-bound ferrisiderophore reductases of Escherichia coli K-12 about?
After uptake of microbial ferrisiderophores, iron is assumed to be released by reduction. Two ferrisiderophore-reductase activities were identified in Escherichia coli K-12. They differed in cellular location, susceptibility to amytal, and competition between oxygen and ferrichrome-iron(III) reduction. The ferrisiderophore reductase associated with the 40,000 X g sediment (membrane-bound enzyme) was inhibited by 10 mM amytal in contrast to the ferrisiderophore reductase present in the 100,000 X g supernatant (soluble enzyme). Reduction by the membrane-bound enzyme followed sigmoid kinetics, but was biphasic in the case of the soluble enzyme. The soluble reductase could be assigned to a protein consisting of a single polypeptide of Mr 26,000. Reduction of iron(III) by the purified enzyme depended on the addition of NADH or NADPH which were equally active reductants. The cofactor FMN and to a lesser degree FAD stimulated the reaction. Substrate specificity of the soluble reductase was low. In addition to the hydroxamate siderophores arthrobactin, schizokinen, fusigen, aerobactin, ferrichrome, ferrioxamine B, coprogen, and ferrichrome A, the iron(III) complexes of synthetic catecholat
Who reads Soluble and membrane-bound ferrisiderophore reductases of Escherichia coli K-12?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Eckhard Fischer; Birgit Strehlow; Dieter Hartz; Volkmar Braun
- Publisher
- Springer; Springer-Verlag; Springer Verlag; Springer Science and Business Media LLC; Archie Comics (ISSN 0302-8933)
- Published
- 1990
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)
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