A reevaluation of iron binding by Mycobactin J

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
Courtney F McQueen, John T Groves

Abstract

The complex stability constant (log β110) and the free iron concentration (pM) are used to compare the relative strength of iron binding by siderophores. Direct measurements of these thermodynamic parameters are often not possible for siderophores due to very large log β110 values ranging from 30 to 50. Instead, siderophore iron(III)-binding constants are determined by competitive experiments with other strong chelators with known values, such as EDTA. Iron(III) binding constants of water-insoluble siderophores, such as the mycobactins produced by the mycobacterium family, have never been directly measured. Since mycobactins contain two hydroxamic acid binding motifs, their log β110 values have been assumed to be comparable to those of other hydroxamate-based siderophores like desferrioxamine B, at ~ 30. However, exochelin MN, another mycobacterial siderophore that contains two hydroxamic acid moieties, has a log β110 of 39.1 and a pM of 31.1, which makes it among the strongest siderophores known. We have found that mycobactin J, the amphiphilic siderophore of Mycobacterium paratuberculosis, can remove iron(III) from TrenCAM (log β110 = 43.6) within 1 min in methanol. This surprising result indicates that log β110 for mycobacti...Continue Reading

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Citations

Feb 6, 2020·Natural Product Reports·Shinichi Nishimura, Nobuaki Matsumori
Oct 6, 2018·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Lawrence Que
Oct 27, 2021·The Journal of Organic Chemistry·Kiat Hwa Chan, John T Groves

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Software Mentioned

TrenCAM
Fuzzy LP Spectral Analyzer

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