Title | Marine amphiphilic siderophores: marinobactin structure, uptake, and microbial partitioning. |
Publication Type | Journal Article |
Year of Publication | 2007 |
Authors | Martinez JS, Butler A |
Journal | J Inorg Biochem |
Volume | 101 |
Issue | 11-12 |
Pagination | 1692-8 |
Date Published | 2007 Nov |
ISSN | 0162-0134 |
Keywords | Cell Membrane, Electrophoresis, Polyacrylamide Gel, Iron, Marinobacter, Molecular Structure, Oligopeptides, Palmitic Acids, Siderophores, Spectrometry, Mass, Electrospray Ionization |
Abstract | Marinobactins A-E are a suite of amphiphilic siderophores which have a common peptidic head group that coordinates Fe(III), and a fatty acid which varies in length and saturation. As a result of the amphiphilic properties of these siderophores it is difficult to study siderophore-mediated uptake of iron, because the amphiphilic siderophores partition indiscriminately in microbial and other membranes. An alternative method to distinguish amphiphilic siderophore partitioning versus siderophore-mediated active uptake for Fe(III)-marinobactin E has been developed. In addition, a new member of the marinobactin family of siderophores is also reported, marinobactin F, which has a C(18) fatty acid with one double bond and which is substantially more hydrophobic that marinobactins A-E. |
DOI | 10.1016/j.jinorgbio.2007.07.007 |
Alternate Journal | J. Inorg. Biochem. |
PubMed ID | 17868890 |
PubMed Central ID | PMC3061822 |
Grant List | GM38130 / GM / NIGMS NIH HHS / United States R01 GM038130-14 / GM / NIGMS NIH HHS / United States R01 GM038130-15 / GM / NIGMS NIH HHS / United States R01 GM038130-16 / GM / NIGMS NIH HHS / United States |