Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter
Transport of vitamin B(12) across the outer membrane of Escherichia coli, like that of iron-siderophore complexes, is an active transport process requiring a specific outer membrane transporter BtuB, the proton motive force, and the trans-periplasmic energy coupling protein TonB. Interaction between...
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| Yayımlandı: | Proc Natl Acad Sci U S A |
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| Asıl Yazarlar: | , |
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
National Academy of Sciences
1999
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC17941/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10485884/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.96.19.10673 |
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