TonB-dependent energy transduction between outer and cytoplasmic membranes

Biometals. 2007 Jun;20(3-4):453-65. doi: 10.1007/s10534-006-9071-6. Epub 2007 Jan 17.

Abstract

The TonB system of Escherichia coli (and most other Gram-negative bacteria) is distinguished by its importance to iron acquisition, its contribution to bacterial pathogenesis, and a unique and mysterious mechanism of action. This system somehow gathers the potential energy of the cytoplasmic membrane (CM) proton gradient and delivers it to active transporters in the outer membrane (OM). Our understanding of this system is confounded by the challenge of reconciling often contradictory in vivo and in vitro studies that are presented in this review.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Biological Transport / physiology
  • Cell Membrane* / metabolism
  • Cell Membrane* / ultrastructure
  • Energy Metabolism
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Escherichia coli* / cytology
  • Escherichia coli* / metabolism
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Sequence Alignment

Substances

  • Escherichia coli Proteins
  • Membrane Proteins
  • tonB protein, E coli