Chemiosmotic Hypothesis of Oxidative Phosphorylation

  title={Chemiosmotic Hypothesis of Oxidative Phosphorylation},
  author={P. Mitchell and J. Moyle},
Dr. Moyle and Dr. Mitchell answer criticisms of their interpretation of tests of the hypothesis proposed by Dr. Mitchell in 1961 to explain ATP synthesis in the inner membrane of mitochondria and of chloroplasts by a fuel-cell type of mechanism 
An evaluation of the Mitchell hypothesis of chemiosmotic coupling in oxidative and photosynthetic phosphorylation.
  • E. C. Slater
  • Medicine, Chemistry
  • European journal of biochemistry
  • 1967
Experimental evidence is presented confirming that, under the conditions of the oxygen-pulse experiments of Mitchell and Moyle, the extrusion of H+ is not associated with the oxidation of mitochondrial NADH, and the respiratory chain included in the chemiosmotic hypothesis is difficult to reconcile with present knowledge of the chain. Expand
The Human OXPHOS System
In this review the composition, structure and function of the complexes of the mammalian mitochondrial electron transport chain and the ATP synthase are highlighted in the context of the ChemiosmoticExpand
Protein and lipid interactions within the respiratory chain : Studies using membrane-mimetic systems
Energy conversion from nutrients to ATP is a vital process in cells. The process, called oxidative phosphorylation (OXPHOS) is performed by a combination of membrane-bound proteins. These proteins ...
Facts and Concepts in Cell Compartmentation
The discovery of intracellular membrane systems in the earliest days of biomedical electron microscopy has since proven to be of prime importance for cell biology and biochemistry. EndomembranesExpand
Molecular motors: What makes ATP synthase spin?
Using sophisticated NMR and chemical probes, one group has uncovered structural changes in a critical subunit that could drive the rotation of the ATP synthase enzyme. Expand
Energy Conservation via Electron-Transferring Flavoprotein in Anaerobic Bacteria
Energy conservation in chemotrophic organisms is generally coupled to redox reactions in catabolic pathways. In the oxidative part or branch, “energy-rich” compounds are formed, from which ATP isExpand
Mitochondria and Aging
Animal cells rely on oxidative phosphorylation to supply the chemical energy necessary for life and this stored energy is coupled to the formation of ATP by the controlled flow of protons down their chemical gradient within complex V, the ATP synthase. Expand
The Mitochondrial Calcium Uniporter (MCU): Molecular Identity and Physiological Roles*
The direct measurement of mitochondrial [Ca2+] with highly specific probes demonstrated that major swings in organellar [Ca2+] parallel the changes occurring in the cytosol and regulate processes asExpand
Keeping mitochondria in shape: a matter of life and death
  • L. Scorrano
  • Biology, Medicine
  • European journal of clinical investigation
  • 2013
Mitochondria are dynamic organelles that participate in energy conversion, metabolism, signaling and apoptosis and are in close contact with the endoplasmic reticulum generating an essential interface in cell physiology and death. Expand
The mitochondrion as Janus Bifrons
The signaling function of mitochondria is considered with a special emphasis on their role in the regulation of redox status of the cell, possibly determining a number of pathologies including cancerExpand


  • P. Mitchell
  • Biology, Medicine
  • Biological reviews of the Cambridge Philosophical Society
  • 1966
The end result of the coupling between the flows through the o/r and h/d pathways in oxidative phosphorylation in mitochondria is that, for the equivalent of each pair of electrons traversing the respiratory chain, up to 3 anhydro-bond equivalents may normally traverse the h/D pathway from adenosine diphosphate plus inorganic phosphate (ADP +Pi) to water. Expand
Stoichiometry of Proton Translocation through the Respiratory Chain and Adenosine Triphosphatase Systems of Rat Liver Mitochondria
Stoichiometry of Proton Translocation through the Respiratory Chain and Adenosine Triphosphatase Systems of Rat Liver Mitochondria shows good correspondence with known proton-proton transfer mechanisms. Expand