Abstract
Cytochrome c oxidase generates a membrane potential and a pH gradient by translocating charges across the membrane in which it is embedded. These gradients inhibit the enzyme in the process of respiratory control. The charge translocation can involve either electrons or protons, the former a consequence of the topochemical arrangement of redox centres, the latter a result of some mechanism of alternating access to the two sides of the membrane by proton-donating and accepting groups, either involving the catalytic machinery of oxygen reduction or an ‘indirect’ conformational process within the protein complex. Respiratory control can be exerted thermodynamically upon the overall process, kinetically upon one or more charge-translocating steps, or allosterically at a non-charge-translocating step, affected by ΔpH and/or Δψ.
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
R. A. Copeland, Confonnational switching at cytochrome a during steady-state turnover of cytochrome coxidase, Proc. Natl. Acad. Sci. USA 88:7281–7283 (1991).
D. Sherman, S. Kotake, N. Ishibe and R. A. Copeland, Resolution of the electronic transitions of cytochrome c oxidase: evidence for two conformational states of ferrous cytochrome a, Proc. Natl. Acad. Sci. USA 88:4265–4269 (1991).
S. R. Lynch, D. Sherman and R. A. Copeland, Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase, J. Biol. Chem. 267:298–302 (1992).
D. Keilin and E. F. Hartree, Cytochrome and cytochrome oxidase, Proc. Roy. Soc. B127:167–191 (1939).
B. C. Hill, The reaction of the electrostatic cytochrome c-cytochrome oxidase complex with oxygen, J. Biol Chem. 266:2219–2226(1991).
S. Han, Y. Ching and D. L. Rousseau, Cytochrome c oxidase: decay of the primary oxygen intermediate involves direct electron transfer from cytochrome a, Proc. Nat. Acad. Sci. 87:8408–8412 (1990).
L. Gregory and S. Ferguson-Miller, Independent control of respiration in cytochrome c oxidase vesicles by pH and electrical gradients, Biochemistry 28:2655–2662 (1989).
S. Papa, N. Capitanio, G. Capitanio, E. De Nitto and M. Minuto, The cytochrome chain of mitochondria exhibits variable H+/e-stoichiometry, FEBS Lett. 288:183–186 (1991).
M. Wikström, Energy-dependent reversal of the cytochrome oxidase reaction, Proc. Natl. Acad. Sci. USA 78:4051–4054 (1981).
M. Wikström, K. Krab and M. Saraste. “Cytochrome Oxidase-A Synthesis,” Academic Press, New York and London (1981).
B. G. Malmström, Cytochrome c oxidase as a redox-linked proton pump, Chem. Rev. 90:1247–1260 (1990).
A. J. Moody, U. Brandt and P. R. Rich, Single electron reduction of ‘slow’ and ‘fast’ cytochrome c oxidase, FEBS Lett. 293:101–105 (1991).
M. Kuboyama, F.C. Yong and T.E. King, Studies on cytochrome oxidase VIII. Preparation and some properties of cardiac cytochrome oxidase, J. Biol. Chem. 247:6375–6383 (1972).
J. M. Wrigglesworth, C.E. Cooper, M. Sharpe and P. Nicholls, The proteoliposomal steady state: effects of size, capacitance and membrane permeability on cytochrome oxidase-induced ion gradients, Bio chem. J. 270:109–118 (1990).
B. Chance and G.R. Williams, The respiratory chain and oxidative phosphorylation, Adv. Enzymol. 17:65–134 (1956).
P. Nicholls and J. M. Wrigglesworth, Routes of cytochrome a3 reduction: the neoclassical model revisited, Ann. N.Y. Acad.Sci. 550:59–67 (1988).
P. Nicholls and V. A. Hildebrandt, Binding of ligands and spectral shifts in cytochrome c oxidase, Bio chem. J. 173:65–72 (1978).
P. Nicholls and L.C. Petersen, Haem-haem interactions in cytochrome aa 3 during the anaerobic-aerobic transition, Biochim. Biophys. Acta 357:462–467 (1974).
M. K. F. Wikström, H. J. Harmon, W. J. Ingledew and B. Chance, A reevaluation of the spectral, potentiometric and energy-linked properties of cytochrome c oxidase in mitochondria, FEBS Lett. 65:259–277 (1976).
G. Goodman and J. S. Leigh, The distance between cytochromes a and a3 in the azide compound of bovine heart cytochrome oxidase, Biochim. Biophys. Acta 890:360–367 (1987).
G. T. Babcock and M. Wikström, Oxygen activation and the conservation of energy in cell respiration,Nature 356:301–309 (1992).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1993 Springer Science+Business Media New York
About this chapter
Cite this chapter
Nicholls, P. (1993). Control of Cytochrome C Oxidase: Kinetic, Thermodynamic or Allosteric?. In: Schuster, S., Rigoulet, M., Ouhabi, R., Mazat, JP. (eds) Modern Trends in Biothermokinetics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2962-0_3
Download citation
DOI: https://doi.org/10.1007/978-1-4615-2962-0_3
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-6288-3
Online ISBN: 978-1-4615-2962-0
eBook Packages: Springer Book Archive