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Chapter 1 : Biochemical and Physical Properties of Siderophores

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Biochemical and Physical Properties of Siderophores, Page 1 of 2

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Abstract:

The significance of iron as a nutrient and its role in biological processes have major consequences in areas of science ranging from geochemistry to human disease. Invading microorganisms exposed to circulating blood produce siderophores to compete for iron with the human transport protein transferrin; this constitutes one aspect of virulence and pathogenicity. This chapter focuses on the coordination chemistry of the remarkable compounds, where a lot of function is packed into small molecules. It summarizes our knowledge of siderophores, a remarkable group of microbial iron-binding molecules. The three broad groups of siderophores (catecholates, hydroxamates, and hydroxycarboxylates) are distinguished by the chemical structure of the metal-binding functionality. The chapter places emphasis on the function, stability, structure, and spectroscopy of siderophores. The basic biochemical and physical properties do much to explain the growing body of biomedical and biochemical science surrounding the siderophores and their iron transport functions.

Citation: Raymond K, Dertz E. 2004. Biochemical and Physical Properties of Siderophores, p 3-17. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch1

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Nuclear Magnetic Resonance Spectroscopy
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Figures

Image of FIGURE 1
FIGURE 1

(Top) Principal functional groups found in siderophores for Fecoordination. The three functional groups are bidentate because each has two oxygen atoms that coordinate iron. (Bottom) The octahedral coordination of Feoccurs by having six ligand atoms in a close-packed geometry around the metal ion. A schematic view of the pseudo-octahedral geometry of Fein siderophores composed of bidentate chelating units (such as hydroxamate and catecholate) is shown. Chirality at the metal centers gives Δ or Λ stereochemistry, and the sequence and orientation of the rings can give a number of geometric numbered isomers. For the Δ complex, the chelates from a right-handed screw around the metal center. A lefthanded screw is found for the Λ complex.

Citation: Raymond K, Dertz E. 2004. Biochemical and Physical Properties of Siderophores, p 3-17. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch1
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Image of FIGURE 2
FIGURE 2

Some representative siderophore structures. The hexadentate siderophores include enterobactin, corynebactin, desferrioxamine B, ferrichrome, pyoverdine, alterobactin, aerobactin, and staphyloferrin A. The tetradentate siderophores include the amonabactins, rhodotorulic acid, and alcaligin. Cepabactin is a bidentate siderophore.

Citation: Raymond K, Dertz E. 2004. Biochemical and Physical Properties of Siderophores, p 3-17. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch1
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Image of FIGURE 3
FIGURE 3

The pM and standard reduction potentials ( ) for representative ferric siderophores and comparison species. Note that the scale is -, such that the reduction potential decreases from bottom to top. While there is a general correlation of with pM, the several large exceptions show that the pM for both ferric and ferrous complexes must be known to predict the potential accurately. The hydroxide potential is calculated using Fe(OH) = 10and Fe(OH) = 10.

Citation: Raymond K, Dertz E. 2004. Biochemical and Physical Properties of Siderophores, p 3-17. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch1
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Image of FIGURE 4
FIGURE 4

The change in pM (pH 7.4; total metal ion concentration, 1 μM) as the total ligand concentration is changed for bidentate (▪), tetradentate (?), and hexadentate (?) complexes of hydroxamate and catecholate siderophores (or analogs). Note the marked increase in sensitivity to concentration for the lower-denticity ligands.

Citation: Raymond K, Dertz E. 2004. Biochemical and Physical Properties of Siderophores, p 3-17. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch1
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Image of FIGURE 5
FIGURE 5

Circular dichroism spectrum of ferric enterobactin in aqueous solution at pH 7.5 in 0.1 M HEPES buffer. The cartoon shows the Δ chirality of the metal center of ferric enterobactin.

Citation: Raymond K, Dertz E. 2004. Biochemical and Physical Properties of Siderophores, p 3-17. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch1
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Image of FIGURE 6
FIGURE 6

One-electron molecular orbital energy level diagram for iron(III) tris (catecholates). The observed charge-transfer transitions are indicated by arrows and are labeled with their corresponding energies in reciprocal centimeters.

Citation: Raymond K, Dertz E. 2004. Biochemical and Physical Properties of Siderophores, p 3-17. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch1
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References

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Tables

Generic image for table
TABLE 1

Comparison of Fe with physiologically relevant cations

Citation: Raymond K, Dertz E. 2004. Biochemical and Physical Properties of Siderophores, p 3-17. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch1
Generic image for table
TABLE 2

Protonation and iron formation constants of representative siderophores

Citation: Raymond K, Dertz E. 2004. Biochemical and Physical Properties of Siderophores, p 3-17. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch1

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