By Toos E. King (auth.), Chong H. Kim, Henry Tedeschi, Joyce J. Diwan, John C. Salerno (eds.)

ISBN-10: 1468486403

ISBN-13: 9781468486407

ISBN-10: 146848642X

ISBN-13: 9781468486421

This publication is formulated from the papers offered on the overseas Symposium on "Membrane Biochemistry and Bioenergetics," held on the Rensselaerville Institute, Rensselaerville, big apple, August 1986, in honor of Tsoo E. King at the celebration of the thirtieth anniversary of reconstitution of arespiratory chain approach by way of Professor David Keilin and Tsoo E. King. Professor Tsoo E. King, to whom this quantity is devoted, has made huge, immense contributions to the sector of isolation and reconstitution of membrane proteins and has persevered to discover the frontiers of bioener­ getics. specifically, his chronic proposals at the life of ubiquinone binding proteins from conceptualization to experimentation ultimately confident many scientists to check those proteins extra . Professor King's coaching of reconstitutively lively succinate dehydrogenase opened a brand new road within the fie1d of membrane bioenergetics, and his paintings has been tremendously favored. the aim of the symposium was once to assemble scientists from varied disciplines on the topic of membrane bioenergetics to debate the hot advancements within the box. This symposium, initiated via the Capital District Bioenergetics crew, used to be attended by way of a hundred scientists, eighty of whom provided their contemporary discoveries. The symposium used to be prepared in a chain of platform lectures, poster displays and dialogue periods in order that all of the contributors had possibilities to debate the themes provided. lots of the members contributed a bankruptcy to this quantity. we wish to specific our remorse to many different scientists together with Professor King's buddies, colleagues and scholars who couldn't attend as a result of a variety of reasons.

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Fiq. Succinate-ubiquinone oxidoreductase translocates hydrogen atoms vectorially from succinate in the aqueous N domain to ubiquinone in the hydrocarbon domain of the membrane (25-28), which is half way across the osmotic barrier for protons. For that reason, it seems appropriate to describe succinate-ubiquinone oxidoreductase as an osmoenzyme. Also, the part of the hydrogen-translocation pathway that involves electron conduction through the iron-sulphur centres must presumably include a parallel pathway of proton conduction (Pre) through the polypeptide system between the flavin prosthetic group of succinate dehydrogenase and the binding site for ubiquinone in QPs.

Pp. 121-134 Japan Scient. Soc. Press, Tokyo. 21. E. (1964) Scient. Amer. 210 (Jan), pp 63-74. 22. E. and Racker, E. (1965) discussion in: Oxidases and Related Redox Systems (eds. ) pp. 1098-1099 (WiJey, New York) 23. J. L. (1971) Science 175, 720-73l. 24. E. (1978) in: Membrane Proteins Vol. 45, 11th FEBS meeting, 1977, eds. P. V. L. J. Moody, pp. 17-31 (Pergamon Press, Oxford) 25. J. and Racker, E. (1972). J. Biol. Chem. 247, 1338-1339. 26. , A1fonzo, M. and Te1ford, J. (1979) Arch. Biochem.

Certain conditions. References and further explanations are in the text. Von Jagow and colleagues extended the b pump concept (79-81) and, in the light of careful measurements of the pH dependence of the midpoint reduction potentials of the high and low potential b cytochromes (bH and b L respectively), applied it to these cytochromes pumping in series, as illustrated (with von Jagow's help) in Fig. 6, C and D. They invoked essentially the same principle of operation of each b cytochrome as in Papa's scheme (Fig.

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Advances in Membrane Biochemistry and Bioenergetics by Toos E. King (auth.), Chong H. Kim, Henry Tedeschi, Joyce J. Diwan, John C. Salerno (eds.)


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