The mechanism of proton transport mediated by mitochondrial uncoupling proteins

FEBS Lett. 1998 Oct 30;438(1-2):10-4. doi: 10.1016/s0014-5793(98)01246-0.


The effort to understand the mechanism of uncoupling by UCP has devolved into two models - the fatty acid protonophore model and the proton buffering model. Evidence for each hypothesis is summarized and evaluated. We also evaluate the obligatory requirement for fatty acids in UCP1-mediated uncoupling and the question of fatty acid affinity for UCP1. The structural bases of UCP transport function and nucleotide inhibition are discussed in light of recent mutagenesis studies and in relationship to the sequences of newly discovered UCPs.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism*
  • Fatty Acids / metabolism*
  • Ion Channels
  • Ion Transport
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Mitochondria / metabolism*
  • Mitochondrial Proteins
  • Molecular Sequence Data
  • Protons*
  • Uncoupling Agents
  • Uncoupling Protein 1


  • Carrier Proteins
  • Fatty Acids
  • Ion Channels
  • Membrane Proteins
  • Mitochondrial Proteins
  • Protons
  • Uncoupling Agents
  • Uncoupling Protein 1