Abstract
The narrow definition of bioenergetics comprises the mechanism by which the energy made available by the oxidation of substrates, or by the absorption of light, is coupled to ‘uphill’ reactions such as the synthesis of ATP from ADP and Pi A broader definition also comprises transport processes. The largest part of ATP synthesis is associated with membrane-bound enzyme complexes found in the plasma membranes of prokaryotes, the inner membrane o mitochondria and the thylakoid membrane of chloroplasts. Despite the different natures of their primary energy sources, these membranes, so-called energy-transducing membranes, have a related evolutionary origin which makes them the core of bioenergetics.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Nicholl DG, Ferguson SJ. In: Bioenergetics 2. Londom: Academic Press, 1992.
Boyer P. A perspective of the binding change mechanism for ATP synthesis. FASEB J 1989; 3:2164–2178.
Pederse PL, Amzel LM. ATP synthases. Structure, reaction center, mechanism, and regulation of nature’s most unique machines. J Biol Chem 1993; 268:9937–9940.
Penefsk HS, Cross RL. Structure and mechanism of F0F1-type ATP synthases and ATPases. Adv Enzymol 1991; 64:173–214.
Tonomur Y. F1-ATPase. In: Energy-transducing ATPases—Structure and kinetics. Avon: Cambridge University Press, 1986:141–183.
Hendersn R, Baldwin JM, Ceska TA et al. Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy. J Mol Biol 1990; 213:899–929.
Dencher NA, Biildt G, Heberle J et al. Light-triggered opening and closing of a hydrophobic gate controls vectorial proton transfer across bacteriorhodopsin. NATO ASI Ser, Ser B 1992; 291:171–185.
Nederkorn PHJ, Timmerman H, Donné-Op den Kelder GM. Does the ternary complex act as a secondary proton pump and a GTP synthase? Trends Pharmacol Sci 1995; 16:156–161.
Krab K, van Wezel J. Improved derivation of phosphate potentials at different temperatures. Biochim Biophys Acta 1992; 1098:172–176.
Slater EC, Rosing J, Mol A. The phosphorylation potential generated by respiring mitochondria. Biochim Biophys Acta 1973; 292:534–553.
Morowiz HJ. Proton semiconductors and energy transduction in biological systems. Am J Physiol 1978; 235:R99–R114.
Nagle F, Tristram-Nagle S. Hydrogen bonded chain mechanisms for proton conduction and proton pumping. J Membrane Biol 1983; 74:1–14.
Nagle F, Morowitz HJ. Molecular mechanisms for proton transport in membranes. Proc Natl Acad Sci USA 1978; 75:298–302.
Iwata, S, Ostermeier C, Ludwig B et al. H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus Denitrificans. Nature 1995; 376:660–669.
Willias RJP. Purpose of proton pathways. Nature 1995; 376:643.
Deamer DW, Nichols JW. Proton flux mechanisms in model and biological membranes. J Membrane Biol 1989; 107:91–103.
Onsage L. In: Whalley E, Jones SJ, Gold LW, eds. Physics and Chemistry of Ice. Ottawa: Royal Society, 1973; 7–12.
Robinsn RA, Stokes RH. In: Electrolyte solutions. 2nd ed. London: Butterworths, 1970.
Nagle F, Mille M. Molecular models of proton pumps. J Chem Phys 1981; 74:1367–137.
Nagle F, Mille M, Morowitz HJ. Theory of hydrogen bonded chains in bioenergetics. J Phys Chem 1980; 72:3959–3971.
Heberl J, Riesle J, Thiedemann G et al. Proton migation along the membrane surface and retarded surface to bulk transfer. Nature 1994; 370:379–382.
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1997 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Nederkoorn, P.H.J., Timmerman, H., den Kelder, G.M.DO. (1997). Bioenergetics. In: Signal Transduction by G Protein-Coupled Receptors. Molecular Biology Intelligence Unit. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1407-3_1
Download citation
DOI: https://doi.org/10.1007/978-1-4684-1407-3_1
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-1409-7
Online ISBN: 978-1-4684-1407-3
eBook Packages: Springer Book Archive