Thermochelin, a Hydroxamate Siderophore from Thermocrispum agreste DSM 44070

Thomas Heine; Marika Mehnert; Rïngo Schwabe; Dirk Tischler

doi:10.4028/www.scientific.net/SSP.262.501

Paper Titles

Molecular Response of the Acidophilic Iron Oxidizer “Ferrovum” sp. JA12 to the Exposure to Elevated Concentrations of Ferrous Iron
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The Surface Chemistry Characterization of Pyrite, Sphalerite and Molybdenite after Bioleaching
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Monitoring of Biofilm Development on Surfaces Using an Electrochemical Method
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EIS Studies of Chalcopyrite Involving Iron(II) Ions
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Thermochelin, a Hydroxamate Siderophore from Thermocrispum agreste DSM 44070
p.501

Siderophore Purification via Immobilized Metal Affinity Chromatography
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Revisiting the Chrome Azurol S Assay for Various Metal Ions
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Gallium Mobilization in Soil by Bacterial Metallophores
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On the Immobilization of Desferrioxamine-Like Siderophores for Selective Metal Binding
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HomeSolid State PhenomenaSolid State Phenomena Vol. 262Thermochelin, a Hydroxamate Siderophore from...

Thermochelin, a Hydroxamate Siderophore from Thermocrispum agreste DSM 44070

Abstract:

Siderophores are produced by microorganisms in iron-deficient environments. They are classified by structure as hydroxamate, catecholate, carboxylate or mixed type siderophores. These differences are also reflected in the selectivity for other valuable elements than iron, which allows designating them as “metallophores”, and makes them of interest for several industrial and medical applications. Thus, it is essential to understand the biosynthesis of these molecules to increase the set of available metallophores that are stable and suited for the respective applications. The probable structure of the metallophore from T. agreste DSM 44070 was predicted by similarity search and gene annotation. An N-hydroxylating monooxygenase (NMO: TheA) of T. agreste DSM 44070 that catalyzes an initial step was synthesized and characterized in detail. The respective metallophore was synthesized, purified and studied. The structure prediction suggested a hydroxamate-type (Erythrochelin-like) metallophore that contains _L-N5-hydroxyornithine. This precursor is synthesized by TheA. The siderophore designated as “Thermochelin” is produced, extracted and purified successfully. Complexation was confirmed by CAS-assay. In this study, we expanded the scope of siderophores and the knowledge towards their biosynthetic pathways. Thermochelin is the second siderophore, which was purified from a thermophilic organism, and TheA is the first NMO, which was characterized from an extremophile.

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Solid State Phenomena (Volume 262)

Pages:

501-504

DOI:

https://doi.org/10.4028/www.scientific.net/SSP.262.501

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Online since:

August 2017

Authors:

Thomas Heine*, Marika Mehnert, Rïngo Schwabe, Dirk Tischler

Keywords:

Hydroxamate, N-Hydroxylating Monooxygenase, Thermochelin, Thermophilic

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References

[1] R.C. Hider, X. Kong, Chemistry and biology of siderophores, Nat. Prod. Rep. 27 (2010) 637-657.

DOI: 10.1039/b906679a

Google Scholar

[2] T.C. Johnstone, E.M. Nolan, Beyond iron: non-classical biological functions of bacterial siderophores, Dalton Trans. (2015) 6320-6339.

DOI: 10.1039/c4dt03559c

Google Scholar

[3] M. Saha, S. Sarkar, B. Sarkar, B.K. Sharma, S. Bhattacharjee, P. Tribedi, Microbial siderophores and their potential applications: a review, Environ. Sci. Pollut. Res. Int. (2016) 3984-3999.

DOI: 10.1007/s11356-015-4294-0

Google Scholar

[4] S.F. Altschul, W. Gish, W. Miller, E.W. Myers, D.J. Lipman, Basic local alignment search tool, J. Mol. Biol. 215 (1990) 403-410.

DOI: 10.1016/s0022-2836(05)80360-2

Google Scholar

[5] S. Kumar, G. Stecher, K. Tamura, MEGA7: Molecular Evolutionary Genetics Analysis Version 7. 0 for Bigger Datasets, Mol. Biol. Evol. 33 (2016) 1870-1874.

DOI: 10.1093/molbev/msw054

Google Scholar

[6] M. Bosello, M. Zeyadi, F.I. Kraas, U. Linne, X. Xie, M.A. Marahiel, Structural characterization of the heterobactin siderophores from Rhodococcus erythropolis PR4 and elucidation of their biosynthetic machinery, J. Nat. Prod. 76 (2013) 2282-2290.

DOI: 10.1021/np4006579

Google Scholar

[7] P. Puigbo, E. Guzman, A. Romeu, S. Garcia-Vallve, OPTIMIZER: a web server for optimizing the codon usage of DNA sequences, Nucleic Acids Res. 35 (2007) W126-W131.

DOI: 10.1093/nar/gkm219

Google Scholar

[8] A. Riedel, T. Heine, A.H. Westphal, C. Conrad, P. Rathsack, W.J.H. van Berkel, D. Tischler, Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding, AMB Express 5 (2015) 1-11.

DOI: 10.1186/s13568-015-0112-9

Google Scholar

[9] L. Ge, S.Y.K. Seah, Heterologous expression, purification, and characterization of an l-ornithine N(5)-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa, J. Bacteriol. 188 (2006) 7205-7210.

DOI: 10.1128/jb.00949-06

Google Scholar

[10] B. Schwyn, J.B. Neilands, Universal chemical assay for the detection and determination of siderophores, Anal. Biochem. 160 (1987) 47-56.

DOI: 10.1016/0003-2697(87)90612-9

Google Scholar

[11] M. Mehnert, R. Schwabe, S. Vater, T. Heine, G. Retamal-Morales, G.J. Levicán, M. Schlömann, D. Tischler, Revisiting the chromeazurol S assay for various metal ions, submitted to Adv. Mat. Res.

DOI: 10.4028/www.scientific.net/ssp.262.509

Google Scholar

[12] L. Robbel, T.A. Knappe, U. Linne, X. Xie, M.A. Marahiel, Erythrochelin a hydroxamate-type siderophore predicted from the genome of Saccharopolyspora erythraea, FEBS J. 277 (2010) 663-676.

DOI: 10.1111/j.1742-4658.2009.07512.x

Google Scholar