Titlebook: Integration of Mitochondrial Function; John J. Lemasters,Charles R. Hackenbrock,Hans V. W Book 1988 Springer Science+Business Media New Yo

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https://doi.org/10.1007/978-1-4899-2551-0ATP; Activation; Amino acid; Aspartat; Calcium; Mammalia; Nucleotide; Vivo; dynamics; enzymes; metabolism; prot

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Diffusion and Collision in Cytochrome ,-Mediated Electron Transportndrial inner membranes have been recently critically reviewed (Hackenbrock et al., 1986). Assessment of the available, pertinent data reveal that all inner membrane redox components are free diffusants and collide at rates sufficient to limit the maximal (uncoupled) rate of electron transport.

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978-1-4899-2553-4Springer Science+Business Media New York 1988

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ATP/2e? Stoichiometries for the Coupling Sites of Mitochondrial Oxidative Phosphorylation: Evaluatiobrane. There remains, however, considerable disagreement as to the proton stoichiometries for these sites as well as for the proton stoichiometries of the proton-translocating ATPase and the various transport systems.

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Nonequilibrium Thermodynamics and Cellular Bioenergeticsthe organism etc. The common denominator to all these energy consuming reactions is to make use of the quality of energy to do work or, in other words, to exploit the possibility of using directed energy rather than randomized thermal motion. Directed energy has been called exergy in contrast to randomized thermal motion which is called entropy..

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The H+/e? Forces and Stoichiometries of the Mitochondrial Respiratory Chainse), (Lawford and Garland, 1973; Di Virgilio and Azzone, 1982); 2H./e. (lq./e.) for site 2 (the cytochrome .. complex), although Pietrobon et al. (1981) have suggested that this may be lower at high Δp; and 0 to 2 H./e. (1 to 3 q./e.) for site 3 (cytochrome oxidase), (Papa et al. 1983, Wikstrom 1977, Reynafarje et al. 1982).