50 years ago Peter Mitchell proposed the chemiosmotic hypothesis for which he was awarded the Nobel Prize for Chemistry in 1978. His comprehensive review on chemiosmotic coupling known as the first "Grey Book", has been reprinted here with permission, to offer an electronic record and easy access to this important contribution to the biochemical literature. This remarkable account of Peter Mitchell's ideas originally published in 1966 is a landmark and must-read publication for any scientist in the field of bioenergetics. As far as was possible, the wording and format of the original publication have been retained. Some changes were required for consistency with BBA formats though these do not affect scientific meaning. A scanned version of the original publication is also provided as a downloadable file in Supplementary Information and can be found online at doi:10.1016/j.bbabio.2011.09.018. See also Editorial in this issue by Peter R. Rich. Original title: CHEMIOSMOTIC COUPLING IN OXIDATIVE AND PHOTOSYNTHETIC PHOSPHORYLATION, by Peter Mitchell, Glynn Research Laboratories, Bodmin, Cornwall, England.

Chemiosmotic coupling in oxidative and photosynthetic phosphorylation

The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy

The inner membranes of mitochondria contain three multi-subunit enzyme complexes that act successively to transfer electrons from NADH to oxygen, which is reduced to water (Fig. I). The first enzyme in the electron transfer chain, NADH:ubiquinone oxidoreductase (or complex I), is the subject of this review. It removes electrons from NADH and passes them via a series of enzyme-bound redox centres (FMN and Fe-S clusters) to the electron acceptor ubiquinone. For each pair of electrons transferred from NADH to ubiquinone it is usually considered that four protons are removed from the matrix (see section 4.1 for further discussion of this point).

https://www.cambridge.org/core/services/aop-cambridge-core/content/view/S003358350000425X

The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.

The microestimation of succinate and the extinction coefficient of cytochrome c.

http://fqb.fcien.edu.uy/docs/PDFS%20teorico%203/Chemiosmotic%20coupling%20in%20oxidative%20and%20photosynthetic%20phosphorylation%20-%20%20Mitchell%20-%201966.pdf

Studies on succinic dehydrogenase. II. Isolation and properties of the dehydrogenase from beef heart.

Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase. vi. further purification and properties of the enzyme from beef heart.

Studies on succinic dehydrogenase. IV. Activation of the beef heart enzyme.

Studies on succinic dehydrogenase. XII. Flavin component of the mammalian enzyme.

Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase. iv. transformation of the dehydrogenase into cytochrome c reductase-diaphorase by the action of acid-ethanol.

Edna B. Kearney

Papers

Studies on succinic dehydrogenase. II. Isolation and properties of the dehydrogenase from beef heart.

Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase. vi. further purification and properties of the enzyme from beef heart.

Studies on succinic dehydrogenase. IV. Activation of the beef heart enzyme.

Studies on succinic dehydrogenase. XII. Flavin component of the mammalian enzyme.

Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase. iv. transformation of the dehydrogenase into cytochrome c reductase-diaphorase by the action of acid-ethanol.