By Valerian E. Kagan, Peter J. Quinn
Due to the fact that its discovery in 1957, Coenzyme Q has piqued the curiosity of scientists from quite a lot of disciplines as a result of its bioenergetics, vitamin-like habit, and interactions with antioxidant supplements E and C. Coenzyme Q: Molecular Mechanisms in wellbeing and fitness and illness is a complete treatise in this often-studied coenzyme. overseas specialists disguise the examine that ended in its emergence as a thrilling, new nutritional supplement.The current quantity summarizes the newest advancements in a number of components of CoQ learn. New ideas on extramitochondrial services of CoQ are mentioned in chapters, whereas contemporary discoveries in biosynthetic pathways for CoQ according to molecular genetic techniques are offered in one other chapter.Further chapters discover the function of CoQ as an antioxidant, revealing the necessity for extra study during this intriguing quarter. This ebook could be of utmost curiosity to biochemists, biophysicists, molecular and mobile biologists, in addition to nutritionists and biomedical medical experts.
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Additional info for Coenzyme Q: Molecular Mechanisms in Health and Disease
Yu, C. , Li, L. , Comparative study of quinone binding proteins in mitochondrial cytochrome b-c1 complex and chloroplast cytochrome b6-f complex, in Highlights in Ubiquinone Research, Lenaz, Barnabei, Rabbi, Battino, Taylor and Francis, London, 1990, 46. 88. Berry, E. A. and Trumpower, B. , Pathways of electrons and protons through the cytochrome bc1 Complex of the mitochondrial respiratory chain, Coenzyme Q, Lenaz, Wiley, Chichester, 1985, 365. 89. , Proton-translocation by membrane-bound NADH: ubiquinone-oxidoreductase (complex I) through redox-gated ligand conduction, Biochim.
If the substrate molecules interact with the active site of the enzyme from within the bilayer, addition of extra lipids to the assay medium increases the value of ␣ by increasing the lipid phase and decreases the substrate concentration (although increasing its total amount) in the lipid phase, resulting in the observation that Kapp increases with an increase in the concentration of total lipid in the assay medium. 5 ROLE OF DIFFUSION IN THE OXIDATIVE PHOSPHORYLATION SYSTEM In the oxidative phosphorylation machinery, diffusion of substrates and substrate-like molecules should play a role in the following compartments: (a) NADϩ/NADH, most substrates for the dehydrogenases, and ADP/ATP in the matrix; (b) ubiquinone in the lipid core of the inner membrane; (c) cytochrome c and glycerol-3-P in the intermembrane space (with glycerol-3-P dehydrogenase being the only primary dehydrogenase with its active site on the cytoplasmic side).
Ragan, C. I. and Cottingham, I. , The kinetics of quinone pools in electron transport, Biochim. Biophys. Acta, 811, 13, 1985. 78. , 311, 107, 1992. 79. , Coenzyme Q deficiency in mitochondria: kinetic saturation versus physical saturation, Molec. , 18, s25–s31, 1997. 80. , Villa, R. , Huertas, J. F. , Fiorella, P. , Genova, M. , 9, 179, 1990. 81. , Nelson, B. , Studies with ubiquinone-depleted submitochondrial particles. Quantitative incorporation of small amounts of ubiquinone and its effects on the NADH and succinate oxidase activities, Eur.