Chemiosmotic Hypothesis of Oxidative Phosphorylation

@article{Mitchell1967ChemiosmoticHO,
  title={Chemiosmotic Hypothesis of Oxidative Phosphorylation},
  author={Peter Mitchell and Jennifer Moyle},
  journal={Nature},
  year={1967},
  volume={213},
  pages={137-139}
}
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 
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 Chemiosmotic
An evaluation of the Mitchell hypothesis of chemiosmotic coupling in oxidative and photosynthetic phosphorylation.
TLDR
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.
Protein and lipid interactions within the respiratory chain : Studies using membrane-mimetic systems
TLDR
Energy conversion from nutrients to ATP is a vital process in cells and a combination of membrane-bound proteins performs this process, called oxidative phosphorylation (OXPHOS), which produces ATP.
Facts and Concepts in Cell Compartmentation
TLDR
Endomembranes completely enclose diverse compartments in eukaryotic cells that, due to their particular respective complements of enzymes, carry out variable metabolic functions.
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 is
Molecular motors: What makes ATP synthase spin?
TLDR
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.
Mitochondria and Aging
TLDR
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.
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 as
Keeping mitochondria in shape: a matter of life and death
  • L. Scorrano
  • Biology
    European journal of clinical investigation
  • 2013
TLDR
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.
Reassessment of the role of ATP in vivo.
...
...

References

SHOWING 1-3 OF 3 REFERENCES
CHEMIOSMOTIC COUPLING IN OXIDATIVE AND PHOTOSYNTHETIC PHOSPHORYLATION
  • P. Mitchell
  • Chemistry
    Biological reviews of the Cambridge Philosophical Society
  • 1966
TLDR
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.
Stoichiometry of Proton Translocation through the Respiratory Chain and Adenosine Triphosphatase Systems of Rat Liver Mitochondria
TLDR
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.