Energy transductions, binding

Crompton, M., McGuinness, O. and Nazareth, W. (1992). The involvement of cyclosporin A binding proteins in regulating and uncoupling mitochondrial energy transduction. Biochim. Biophys. Acta. 1101, 214. 

In a series of papers, we have proposed the torsional mechanism of energy transduction and ATP synthesis, the only unified and detailed molecular mechanism of ATP synthesis to date [16-20,56] which addresses the issues of ion translocation in Fq [16, 20, 56], ionmotive torque generation in Fq [16, 20, 56], torque transmission from Fq to Fj [17,18], energy storage in the enzyme [17], conformational changes in Fj [18], and the catalytic cycle of ATP synthesis [18, 19]. We have also studied the thermodynamic and kinetic aspects of ATP synthesis [19,20,41,42,56]. A kinetic scheme has been developed and mathematically analyzed to obtain a kinetic model relating the rate of ATP synthesis to pHjn and pH m in the Fq portion and the adenine nucleotide concentrations in the Fj portion of ATP synthase. Analysis of these kinetic models reveals a wealth of mechanistic details such as the absence of cooperativity in the Fj portion of ATP synthase, order of substrate binding and product release events, and kinetic inequivalence of ApH and Aip. 

Fig. 11. Q-cycle model (A) Location of Cyt in the thylakoid membrane (B) Enlarged model of the Cyt b f complex showing the quinone binding sites Qo and Qr as well as the redox components Cyt be, R-[2Fe-2S], and Cyt f along with symbols for indicating their redox states. (C) Sequence of electron and proton transfers. See text for details. It Is assumed that the Initial redox state of the system has been conditioned by the photochemical oxidation of P700 in the PS-I reaction center. (C) adapted from Cramer and Knaff (1990) Energy Transduction in Bioiogical Membranes, p 343. Springer.

Pedersen, P. A., Jorgensen, J. K,, and Jorgensen, P. L. 2000. Importance ofeonserved a-subunil TiDGVND for Vlg binding, pliospho lylation, energy transduction in Na, K A4 Pase. J. Biol. Chem 275 37588 37.595. 

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