PMID- 12765765
OWN - NLM
STAT- MEDLINE
DCOM- 20030711
LR  - 20220330
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1604
IP  - 2
DP  - 2003 Jun 5
TI  - Intrinsic and extrinsic uncoupling of oxidative phosphorylation.
PG  - 77-94
AB  - This article reviews parameters of extrinsic uncoupling of oxidative 
      phosphorylation (OxPhos) in mitochondria, based on induction of a proton leak 
      across the inner membrane. The effects of classical uncouplers, fatty acids, 
      uncoupling proteins (UCP1-UCP5) and thyroid hormones on the efficiency of OxPhos 
      are described. Furthermore, the present knowledge on intrinsic uncoupling of 
      cytochrome c oxidase (decrease of H(+)/e(-) stoichiometry=slip) is reviewed. 
      Among the three proton pumps of the respiratory chain of mitochondria and 
      bacteria, only cytochrome c oxidase is known to exhibit a slip of proton pumping. 
      Intrinsic uncoupling was shown after chemical modification, by site-directed 
      mutagenesis of the bacterial enzyme, at high membrane potential DeltaPsi, and in 
      a tissue-specific manner to increase thermogenesis in heart and skeletal muscle 
      by high ATP/ADP ratios, and in non-skeletal muscle tissues by palmitate. In 
      addition, two mechanisms of respiratory control are described. The first occurs 
      through the membrane potential DeltaPsi and maintains high DeltaPsi values 
      (150-200 mV). The second occurs only in mitochondria, is suggested to keep 
      DeltaPsi at low levels (100-150 mV) through the potential dependence of the ATP 
      synthase and the allosteric ATP inhibition of cytochrome c oxidase at high 
      ATP/ADP ratios, and is reversibly switched on by cAMP-dependent phosphorylation. 
      Finally, the regulation of DeltaPsi and the production of reactive oxygen species 
      (ROS) in mitochondria at high DeltaPsi values (150-200 mV) are discussed.
FAU - Kadenbach, Bernhard
AU  - Kadenbach B
AD  - Fachbereich Chemie, Philipps-Universitat, Hans-Meerwein-Strasse, D-35032 Marburg, 
      Germany. Kadenbach@chemie.uni-marburg.de
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Fatty Acids)
RN  - 0 (Membrane Proteins)
RN  - 0 (Proton Pumps)
RN  - 0 (Protons)
RN  - 0 (Reactive Oxygen Species)
RN  - 0 (Thyroid Hormones)
RN  - 0 (Uncoupling Agents)
RN  - 61D2G4IYVH (Adenosine Diphosphate)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - EC 3.6.3.14 (Proton-Translocating ATPases)
SB  - IM
MH  - Adenosine Diphosphate/metabolism
MH  - Adenosine Triphosphate/metabolism
MH  - Animals
MH  - Biological Evolution
MH  - Electron Transport Complex IV/metabolism
MH  - Energy Metabolism
MH  - Fatty Acids/metabolism
MH  - Intracellular Membranes/metabolism
MH  - Membrane Potentials
MH  - Membrane Proteins/metabolism
MH  - Mitochondria/drug effects/metabolism
MH  - Models, Biological
MH  - *Oxidative Phosphorylation/drug effects
MH  - Proton Pumps/drug effects/metabolism
MH  - Proton-Translocating ATPases/metabolism
MH  - Protons
MH  - Reactive Oxygen Species/metabolism
MH  - Thyroid Hormones/metabolism
MH  - Uncoupling Agents/*metabolism/pharmacology
RF  - 209
EDAT- 2003/05/27 05:00
MHDA- 2003/07/12 05:00
CRDT- 2003/05/27 05:00
PHST- 2003/05/27 05:00 [pubmed]
PHST- 2003/07/12 05:00 [medline]
PHST- 2003/05/27 05:00 [entrez]
AID - S0005272803000276 [pii]
AID - 10.1016/s0005-2728(03)00027-6 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2003 Jun 5;1604(2):77-94. doi: 
      10.1016/s0005-2728(03)00027-6.