Animals microbial iron transport

Microbial iron transport and infections in animals and plants 679... 

B. F. Matzanke, Mossbauer Spectroscopy of Microbial Iron Uptake and Metabolism, in Iron Transport in Microbes, Plants and Animals , eds. G. Winkehnann, D. van der Helm, and J. B. Neilands, VCH, Weinheim, 1987, p. 251. 

The structure and function of lactoferrin (Lf) have been extensively reviewed,and will not be covered here in detail. These proteins retain iron to a much lower pH than serum transferrins absence of the pH-sensitive dilysine trigger (see below) enhances the add stability of ferric Lf. " Retention of iron provides a bacteriostatic environment, highly effective in limiting microbial growth. A highly cationic molecule, Lf also binds anions such as DNA and heparin. Despite high sequence identity (60%) between sTf and Lf, the major function of Lf does not appear to be iron transport. While a variety of mammalian cells express receptors for Lf, the function of Lf for those cells is still not well defined. " A recent (2001) crystal structure indicates that Lf may be involved with the polymerization of melanin monomers, proteins responsible for the coloration of animal skin and hair. " ... 

As metal chelating agents, sideramines fulfil two functions they transport iron into the microbial cell and/or make the chelated iron available for heme synthesis. In analogy with animal transferrin, the iron of microbial ferrichrome is transferred enzymatically into the porphyrin molecule during heme synthesis. 

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