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Article

Ferric hydroxamate binding protein FhuD from Escherichia coli: mutants in conserved and non-conserved regions.

Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine - 1 Jun 2002

Clarke Teresa E, Rohrbach Martin R, Tari Leslie W, Vogel Hans J, Köster Wolfgang

Abstract excerpt

Uptake of iron complexes into the gram-negative bacterial cell requires highly specific outer membrane receptors and specific ATP-dependent (ATP-Binding-Cassette (ABC)) transport systems located in the inner membrane. The latter type of import system is characterized by a periplasmic binding protein (BP), integral membrane proteins, and membrane-associated ATP-hydrolyzing proteins. In gram-positive bacteria...

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Identifiers

PMID: 12046920
DOI: 10.1023/a:1015249530156

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Ferric hydroxamate binding protein FhuD from Escherichia coli: mutants in conserved and non-conserved regions.PMID 12046920Read ↗

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Point mutations in two conserved glycine residues within the integral membrane protein FhuB affect iron(III) hydroxamate transport.Semantic proximity Read ↗

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