The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli
Open accessAbstract
Cells of Escherichia coli pump cobalamin (vitamin B12) across their outer membranes into the periplasmic space, and it was concluded previously that this process is potentiated by the proton motive force of the inner membrane. The novelty of such an energy coupling mechanism and its relevance to other outer membrane transport processes have required confirmation of this conclusion by studies with cells in which cobalamin transport is limited to the outer membrane. Accordingly, I have examined the effects of cyanide and of 2,4-dinitrophenol on cobalamin uptake in btuC and atp mutants, which lack inner membrane cobalamin transport and the membrane-bound ATP synthase, respectively. Dinitrophenol eliminated cobalamin transport in all strains, but cyanide inhibited this process only in atp and btuC atp mutant cells, providing conclusive evidence that cobalamin transport across the outer membrane requires specifically the proton motive force of the inner membrane. The coupling of metabolic energy to outer membrane cobalamin transport requires the TonB protein and is stimulated by the ExbB protein. I show here that the tolQ gene product can partly replace the function of the ExbB protein. Cells with mutations in both exbB and tolQ had no measurable cobalamin transport and thus had a phenotype that was essentially the same as TonB-. I conclude that the ExbB protein is a normal component of the energy coupling system for the transport of cobalamin across the outer membrane.
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Bacterial Iron Sources: From Siderophores to Hemophores
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Metadata
- Authors
- Bradbeer, C.
- Affiliations
- University of Virginia (US)
- Corresponding author
- Bradbeer, C
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1993-05
- Volume
- 175
- Issue
- 10
- Pages
- 3146-3150
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC204637
- OpenAlex
- W1912992879
- Cited by
- 188
- References
- 26
- Citations by year
- 2026: 3 · 2024: 3 · 2023: 5 · 2022: 5 · 2021: 8 · 2020: 3 · 2019: 3 · 2018: 1 · 2017: 2 · 2016: 6 · 2015: 3 · 2014: 6 · 2013: 7 · 2012: 4
- FWCI
- 4.84
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Bacteriology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- cobalamin uptake, vitamin B12, outer membrane transport, proton motive force, Escherichia coli, TonB, ExbB, TolQ, 2,4-dinitrophenol, cyanide, energy coupling, periplasmic transport
- MeSH terms
- Bacterial Proteins, Biological Transport, Active, Cell Membrane, Cyanides, Dinitrophenols, Escherichia coli, Proton-Translocating ATPases, Membrane Proteins, Protons, Transduction, Genetic, Vitamin B 12, Mutagenesis, ATP-Binding Cassette Transporters, 2,4-Dinitrophenol, Escherichia coli Proteins
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