A Versatile Synthesis of Deferrioxamine B

1995 ◽  
Vol 60 (1) ◽  
pp. 109-114 ◽  
Author(s):  
Raymond J. Bergeron ◽  
James S. McManis ◽  
Otto IV Phanstiel ◽  
J. R. Timothy Vinson
Keyword(s):  
Deferrioxamine B

scholarly journals Degradation Pathway and Generation of Monohydroxamic Acids from the Trihydroxamate Siderophore Deferrioxamine B

2004 ◽  
Vol 70 (2) ◽  
pp. 831-836 ◽  
Author(s):  
Agnes Pierwola ◽  
Tomasz Krupinski ◽  
Peter Zalupski ◽  
Michael Chiarelli ◽  
Domenic Castignetti
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
High Performance ◽  
Degradation Pathway ◽  
Ferric Ion ◽  
Mesorhizobium Loti ◽  
Enzyme Preparations ◽  
Carbon And Nitrogen ◽  
Deferrioxamine B ◽  
Hydroxamate Siderophores

ABSTRACT Siderophores are avid ferric ion-chelating molecules that sequester the metal for microbes. Microbes elicit siderophores in numerous and different environments, but the means by which these molecules reenter the carbon and nitrogen cycles is poorly understood. The metabolism of the trihydroxamic acid siderophore deferrioxamine B by a Mesorhizobium loti isolated from soil was investigated. Specifically, the pathway by which the compound is cleaved into its constituent monohydroxamates was examined. High-performance liquid chromatography and mass-spectroscopy analyses demonstrated that M. loti enzyme preparations degraded deferrioxamine B, yielding a mass-to-charge (m/z) 361 dihydroxamic acid intermediate and an m/z 219 monohydroxamate. The dihydroxamic acid was further degraded to yield a second molecule of the m/z 219 monohydroxamate as well as an m/z 161 monohydroxamate. These studies indicate that the dissimilation of deferrioxamine B by M. loti proceeds by a specific, achiral degradation and likely represents the reversal by which hydroxamate siderophores are thought to be synthesized.

Evidence that a deferrioxamine B degrading enzyme is a serine protease

1998 ◽  
Vol 44 (6) ◽  
pp. 521-527 ◽  
Author(s):  
Ninef Zaya ◽  
Alexandra Roginsky ◽  
Jamila Williams ◽  
Domenic Castignetti
Keyword(s):  
Catalytic Activity ◽  
Serine Protease ◽  
Calcium Ions ◽  
Ferric Ion ◽  
Plant Interactions ◽  
Degrading Enzyme ◽  
Carbon And Nitrogen ◽  
Serine Peptidase ◽  
Deferrioxamine B ◽  
Low Concentrations

Siderophores are organic biomolecules synthesized by a wide variety of microbes. The molecules sequester ferric ion from environments where it is present at extremely low concentrations. Siderophores are of consequence with respect to microbial nutrition, pathogenicity, virulence, and microbe-plant interactions. How siderophores are degraded and returned to the carbon and nitrogen cycles is not well understood. The catalytic activity of an enzyme from a bacterium that degrades the siderophore deferrioxamine B has been examined. While the degradation of deferrioxamine B is sensitive to sulfhydryl and metal moiety inhibitors, the data presented is most consistent with the hypothesis that the enzyme uses a hydroxyl moiety (serine peptidase) to catalyze the degradation of deferrioxamine B. If sulfhydryl and metal inhibitors are simultaneously present at concentrations that when alone only partially inhibit the enzyme, the enzyme is unable to catalyze deferrioxamine B dissimilation. Analysis of the inhibitor experiments conducted led to the conclusion that the deferrioxamine B degrading enzyme is a serine-peptidase-like enzyme that needs calcium ions and sulfhydryl groups to be fully activated or stabilized. The knowledge of the catalytic moieties of the enzyme will be exploited to purify the enzyme.Key words: siderophores, deferrioxamine B, siderophore degradation.

scholarly journals Draft Genome Sequence of the Siderophore-Degrading Soil Bacterium Mesorhizobium loti Strain LU

2018 ◽  
Vol 6 (6) ◽  
pp. e00029-18
Author(s):  
Domenic Castignetti ◽  
Nathaniel Polley ◽  
Catherine Putonti
Keyword(s):  
Genome Size ◽  
Genome Sequence ◽  
Draft Genome ◽  
Gc Content ◽  
Soil Bacterium ◽  
Draft Genome Sequence ◽  
Mesorhizobium Loti ◽  
Deferrioxamine B

ABSTRACTHere, we present the draft genome of Mesorhizobium loti strain LU, a soil bacterium capable of degrading the trihydroxamate siderophore deferrioxamine B to its constituent monohydroxamic acids. Genome size was 6,399,828 bp, with a GC content of 61.5%. This draft genome consists of 35 scaffolds, with an N50 of 389,921 bp.

Cellular pharmacology of deferrioxamine B and derivatives in cultured rat hepatocytes in relation to iron mobilization

1985 ◽  
Vol 34 (8) ◽  
pp. 1175-1183 ◽  
Author(s):  
Ruth Laub ◽  
Yves-Jacques Schneider ◽  
Jean-Noël Octave ◽  
André Trouet ◽  
Robert R. Crichton
Keyword(s):  
Rat Hepatocytes ◽  
Iron Mobilization ◽  
Cellular Pharmacology ◽  
Deferrioxamine B ◽  
Cultured Rat Hepatocytes

The catabolism and heterotrophic nitrification of the siderophore deferrioxamine B

1990 ◽  
Vol 3 (3-4) ◽  
pp. 197-203 ◽  
Author(s):  
Domenic Castignetti ◽  
Abdul S. Siddiqui
Keyword(s):  
Heterotrophic Nitrification ◽  
Deferrioxamine B
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