Marine amphiphilic siderophores: marinobactin structure, uptake, and microbial partitioning.

TitleMarine amphiphilic siderophores: marinobactin structure, uptake, and microbial partitioning.
Publication TypeJournal Article
Year of Publication2007
AuthorsMartinez JS, Butler A
JournalJ Inorg Biochem
Volume101
Issue11-12
Pagination1692-8
Date Published2007 Nov
ISSN0162-0134
KeywordsCell 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.

DOI10.1016/j.jinorgbio.2007.07.007
Alternate JournalJ. Inorg. Biochem.
PubMed ID17868890
PubMed Central IDPMC3061822
Grant ListGM38130 / 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