Domain preference in iron removal from human transferrin by the bacterial siderophores aerobactin and enterochelin
- 1 December 1988
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 178 (2), 477-481
- https://doi.org/10.1111/j.1432-1033.1988.tb14473.x
Abstract
The ability of the siderophores aerobactin and enterochelin to remove iron from transferrin is reported. Aerobactin removes iron from both high-affinity sites on the transferrin molecule, but shows a marked preference for the C-terminal site. This preference is different to that of many iron chelators. Enterochelin removes iron perferentially from the N-terminal site. No evidence for synergism between aerobactin and bidentate ligands could be detected.This publication has 37 references indexed in Scilit:
- Molecular structure of serum transferrin at 3.3-.ANG. resolutionBiochemistry, 1988
- The effect of pH on the kinetics of iron release from diferric ovotransferrin induced by pyrophosphateJournal of Inorganic Biochemistry, 1987
- Site specificity of iron removal from transferrin by α‐ketohydroxypyridine chelatorsFEBS Letters, 1985
- Microbial Envelope Proteins Related to IronAnnual Review of Microbiology, 1982
- The effect of salts on the kinetics of iron release from N-terminal and C-terminal monoferrictransferrinsBiochemical and Biophysical Research Communications, 1981
- Binding of iron from nitrilotriacetate analogs by human transferrinBiochemistry, 1980
- Coordination chemistry of microbial iron transport compounds. 19. Stability constants and electrochemical behavior of ferric enterobactin and model complexesJournal of the American Chemical Society, 1979
- Ferric ion sequestering agents. 2. Kinetics and mechanism of iron removal from transferrin by enterobactin and synthetic tricatecholsJournal of the American Chemical Society, 1979
- ENTEROBACTERIAL CHELATORS OF IRON: THEIR OCCURRENCE, DETECTION, AND RELATION TO PATHOGENICITYJournal of Medical Microbiology, 1975
- The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62-1Biochimica et Biophysica Acta (BBA) - General Subjects, 1969