Disease relevance of

• The FhuE protein of Escherichia coli functions as the receptor for ferric coprogen and ferric-rhodotorulic acid [1].
• Iron from exogenous chelates, e.g., from coprogen produced by Neurospora crassa for ferrioxamine B produced by Streptomyces pilosus, can obviously not be taken up by Aspergillus, confirming the pronounced specificity of chelate-iron transport in fungi [2].
• Localization of functional domains in the Escherichia coli coprogen receptor FhuE and the Pseudomonas putida ferric-pseudobactin 358 receptor PupA [3].

High impact information on

• Structures of FhuD complexed with the antibiotic albomycin, the fungal siderophore coprogen and the drug Desferal have been determined at high resolution by x-ray crystallography [4].
• Coprogen is made mainly in the liver and is excreted predominantly in the feces [5].
• Removal of iron from coprogen, ferrichrome, and ferrioxamine B was significantly lower in fhuF mutants compared to the corresponding parental strains, which suggested that FhuF is involved in iron removal from these hydroxamate-type siderophores [6].
• A redox potential E(1/2) of -310 +/- 25 mV relative to the normal hydrogen electrode was determined for FhuF by EPR redox titration; this redox potential is sufficient to reduce the siderophores coprogen and ferrichrome [6].
• The possible involvement of the mitochondrial peripheral-type benzodiazepine receptor (M-PBR) in Coprogen transport into mitochondria is discussed [7].

Chemical compound and disease context of

• Identification of an iron uptake system specific for coprogen and rhodotorulic acid in Escherichia coli K12 [8].

Biological context of

• The results indicate that coprogen hydrolysis products are an excellent source for Fe nutrition of plants [9].
• A complete cDNA clone encoding human coproporphyrinogen (coprogen) oxidase, the sixth enzyme in the heme biosynthetic pathway, has been isolated from a human placenta cDNA library [10].
• Chiral linear hydroxamates as biomimetic analogues of ferrioxamine and coprogen and their use in probing siderophore-receptor specificity in bacteria and fungi [11].

Anatomical context of

• In this work, the conversion of ALA to Coprogen in the cytoplasm of MLA 144 cells (a retrovirally transformed gibbon ape leukemic T cell line) is demonstrated [7].

Associations of with other chemical compounds

• In short term experiments radioactive iron uptake and translocation rates were determined using ferrioxamine B, coprogen and hydrolysis products of coprogen [9].
• Iron reduction assays using cucumber roots or ascorbic acid also showed that iron bound to hydrolysis products of coprogen was more easily reduced compared to iron bound to trihydroxamates [9].
• Resistance of FhuD to proteinase K in the presence of ferrichrome, aerobactin, and coprogen indicated binding of these substrates to FhuD [12].

Gene context of

• In addition to fhueE the genes fhuCDB, tonB and exbB were necessary for iron coprogen uptake [8].
• Iron(III) chelates of nineteen trihydroxamate siderophores of fungal origin, including ferrichromes, coprogen and triacetylfusarinine C, were separated on a preparative scale with a reversed-phase column using the octadecyl silica gels LRP-1 or LRP-2 as the stationary phase and a water-methanol gradient as the mobile phase [13].
• The fhuE mutant was sensitive to iron starvation and defective in coprogen-mediated iron uptake [14].
• Hybrid proteins that contained at least the amino-terminal 516 amino acids of mature FhuE were active as a receptor for coprogen and interacted with the E. coli TonB protein [3].
• In this paper, we show that chimeric proteins consisting of the central part of FhuA and the N- and C-terminal parts of FhuE (coprogen receptor) or the N- and/or C-terminal parts of FoxA (ferrioxamine B receptor), function as ferrichrome transport proteins [15].

References