The mechanism of proton transport mediated by mitochondrial uncoupling proteins.
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.
Garlid
K D
KD
Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland 97291-1000, USA. garlid@bmb.ogi.edu
Jabůrek
M
M
Jezek
P
P
D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D005227:Fatty Acids / Q000378:metabolism*; D007473:Ion Channels; D017136:Ion Transport; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism*; D024101:Mitochondrial Proteins; D008969:Molecular Sequence Data; D011522:Protons; D014475:Uncoupling Agents; D000071256:Uncoupling Protein 1
D002352:Carrier Proteins; D005227:Fatty Acids; D007473:Ion Channels; D008565:Membrane Proteins; D024101:Mitochondrial Proteins; D011522:Protons; D014475:Uncoupling Agents; D000071256:Uncoupling Protein 1