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Science 23 May 1997:
Vol. 276. no. 5316, pp. 1261 - 1264
DOI: 10.1126/science.276.5316.1261
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Reports

Ligand-Specific Opening of a Gated-Porin Channel in the Outer Membrane of Living Bacteria

Xunqing Jiang, Marvin A. Payne, Zhenghua Cao, Samuel B. Foster, Jimmy B. Feix, Salete M. C. Newton, Phillip E. Klebba *

Ligand-gated membrane channels selectively facilitate the entry of iron into prokaryotic cells. The essential role of iron in metabolism makes its acquisition a determinant of bacterial pathogenesis and a target for therapeutic strategies. In Gram-negative bacteria, TonB-dependent outer membrane proteins form energized, gated pores that bind iron chelates (siderophores) and internalize them. The time-resolved operation of the Escherichia coli ferric enterobactin receptor FepA was observed in vivo with electron spin resonance spectroscopy by monitoring the mobility of covalently bound nitroxide spin labels. A ligand-binding surface loop of FepA, which normally closes its transmembrane channel, exhibited energy-dependent structural changes during iron and toxin (colicin) transport. These changes were not merely associated with ligand binding, but occurred during ligand uptake through the outer membrane bilayer. The results demonstrate by a physical method that gated-porin channels open and close during membrane transport in vivo.

X. Jiang, M. A. Payne, Z. Cao, S. B. Foster, P. E. Klebba, Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019, USA.
J. B. Feix, ESR Center of the Biophysics Research Institute, Medical College of Wisconsin, Milwaukee, WI 53226, USA.
S. M. C. Newton, Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019, USA, and Departamento de Microbiologia, Universidade de São Paulo, São Paulo, Brazil.
*   To whom correspondence should be addressed. E-mail: peklebba{at}chemdept.chem.uoknor.edu

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