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Review
. 2009 Oct;109(10):4580-95.
doi: 10.1021/cr9002787.

Microbial iron acquisition: marine and terrestrial siderophores

Moriah Sandy  1 , Alison Butler
Affiliations
Review

Microbial iron acquisition: marine and terrestrial siderophores

Moriah Sandy et al. Chem Rev. 2009 Oct.
No abstract available

PubMed Disclaimer

Figures

Figure 1
Figure 1
Microbial (Gram negative) iron uptake pathways.
Figure 2
Figure 2
Ribbon diagrams of outer membrane siderophore receptor proteins from E. coli: ferric-citrate (FecA), ferric-enterobactin (FepA) and ferric-hydroxamate (FhuA); and P. aeruginosa: ferric pyoverdine (FpvA) and ferric pyochelin (FptA).
Figure 3
Figure 3
Schematic of the proteins involved in ferrichrome transport. The crystal structure of FhuA in complex with the C-terminus of TonB was reported by Pawelek et al, 2006.
Figure 4
Figure 4
Ribbon representation of the S. marcescens hemophore, HasA (red), bound to its outer membrane receptor protein HasR (blue) (PDB code 3CSN).
Figure 5
Figure 5
Ribbon diagram depiction of the Haemophilus influenza Fbp protein, the ferric binding site is shown on the right. The ferric ion is coordinated by two oxygens from Tyr195 and Tyr196, an imidazole nitrogen from His9, a carboxylate oxygen from Glu57, an oxygen atom from an exogeneous phosphate anion, and an oxygen atom from a water molecule in an octahedral arrangement. (PDB Code 1MRB)
Figure 6
Figure 6
Crystal structure of the ferric uptake regulator (Fur) protein from Vibrio cholerae.
Figure 7
Figure 7
Structures of enterobactin, salmochelin S4 and bacillibactin.
Figure 8
Figure 8
Structures of desferrioxamines E, G and B.
Figure 9
Figure 9
Structures of selected α-hydroxycarboxylate siderophores.
Figure 10
Figure 10
Suites of marine amphiphilic siderophores: marinobactins (Marinobacter sp. DS40M6)- and aquachelins (Halomonas aquamarina DS40M3); amphibactins (Vibrio sp. R10); loihichelins (Halomonas sp. LOB-5); ochrobactins (Ochrobactrum sp. SP18); synechobactins (Synechococcus sp. PCC 7002).
Figure 11
Figure 11
Coordination of Fe(III) could give ME a larger head group area : tail volume ratio such that a smaller micelle is formed. Reproduced from reference 107.
Figure 12
Figure 12
Multilamellar vesicle formation from Fe(III)-marinobactin E induced by addition of Zn(II), Cd(II), La(III) or excess Fe(III). Adapted from reference.
Figure 13
Figure 13
Proposed terminal carboxylate crosslinking of marinobactin E by the added cations, M (Zn(II), Cd(II), La(III) or excess Fe(III)). The bis-bidentate coordination geometry of the two carboxylates shown in the figure could also be bis-monodentate carboxylate cross linking. The resulting “composite surfactant” would have a lower headgroup-area : tail-volume ratio that may favor vesicle formation. “L” is an undefined ligand to fill out the octahedral coordination.
Figure 14
Figure 14
Reaction scheme for the uv photolysis of Fe(III)-aerobactin under aerobic conditions.
Figure 15
Figure 15
Photoreaction of Fe(III)-vibrioferrin. Reaction derived from data presented in reference 120.
Figure 16
Figure 16
Proposed photoreaction of diferric dicitrate in acid. Reaction derived from data presented in reference 114.
Figure 17
Figure 17
Photoreaction of Fe(III)-aquachelin. “L” is an undefined ligand to fill out the octahedral coordination.
Figure 18
Figure 18
Structures of other marine peptide siderophores that contain β-hydroxyaspartic acid.
Figure 19
Figure 19
Other siderophores produced by marine pathogens and oceanic bacteria: petrobactin, petrobactin-(SO3H), and petrobactin-(SO3H)2 (M hydrocarbonoclasticus, Marinobacter aquaeolei VT8);,, vanchrobactin and anguibactin (Vibrio anguillarum);, amonabactins (Aeromonas hydrophila).
Figure 20
Figure 20
Structures of the ornibactins and corrugatin.
Figure 21
Figure 21
Comparison of the amphiphilic citrate siderophores of acinetoferrin rhizobactin 1021 and the synechobactins to the hydrophilic schizokinen siderophore.
Figure 22
Figure 22
Structures of mycobactins and carboxymycobactins produced by Mycobacteria.
Figure 23
Figure 23
Multiple siderophores produced by different pathogenic bacteria: enterobactin,, salmochelins, aerobactin,, and yersinabactin (E. coli, Salmonella, and Yersinia sp.); bacillibactin and petrobactin (Bacillus sp.); pyochelin and pyoverdin (P. aeruginosa); chrysobactin and achromobactin (E. chrysanthemi).,
Figure 24
Figure 24
Ribbon representation of siderocalin bound to ferric enterobactin (PDB code 3BYO).
See this image and copyright information in PMC

References

    1. Crosa JH, Mey AR, Payne SM, editors. Iron Transport In Bacteria. ASM Press; Washington DC: 2004.
    1. Templeton DM, editor. Molecular and Cellular Iron Transport. Marcel Dekker, Inc.; New York: 2002.
    1. Martin JH, Gorden RM. Deep Sea Research. 1988;35:117.
    1. Aguilar-Islas AM, Hurst MP, Buck KN, Sohst B, Smith GJ, Lohan MC, Bruland KW. Progress in Oceanography. 2007;73:99.
    1. Rue EL, Bruland KW. Mar Chem. 1995;50:117.

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