Alternative oxidase in the branched mitochondrial respiratory network: an overview on structure, function, regulation, and role

Braz J Med Biol Res. 1998 Jun;31(6):733-47. doi: 10.1590/s0100-879x1998000600003.

Abstract

Plants and some other organisms including protists possess a complex branched respiratory network in their mitochondria. Some pathways of this network are not energy-conserving and allow sites of energy conservation to be bypassed, leading to a decrease of the energy yield in the cells. It is a challenge to understand the regulation of the partitioning of electrons between the various energy-dissipating and -conserving pathways. This review is focused on the oxidase side of the respiratory chain that presents a cyanide-resistant energy-dissipating alternative oxidase (AOX) besides the cytochrome pathway. The known structural properties of AOX are described including transmembrane topology, dimerization, and active sites. Regulation of the alternative oxidase activity is presented in detail because of its complexity. The alternative oxidase activity is dependent on substrate availability: total ubiquinone concentration and its redox state in the membrane and O2 concentration in the cell. The alternative oxidase activity can be long-term regulated (gene expression) or short-term (post-translational modification, allosteric activation) regulated. Electron distribution (partitioning) between the alternative and cytochrome pathways during steady-state respiration is a crucial measurement to quantitatively analyze the effects of the various levels of regulation of the alternative oxidase. Three approaches are described with their specific domain of application and limitations: kinetic approach, oxygen isotope differential discrimination, and ADP/O method (thermokinetic approach). Lastly, the role of the alternative oxidase in non-thermogenic tissues is discussed in relation to the energy metabolism balance of the cell (supply in reducing equivalents/demand in energy and carbon) and with harmful reactive oxygen species formation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Cell Respiration
  • Cyanides
  • Electron Transport
  • Mitochondria / enzymology*
  • Mitochondrial Proteins
  • Oxidoreductases / physiology*
  • Plant Proteins
  • Plants / metabolism*

Substances

  • Cyanides
  • Mitochondrial Proteins
  • Plant Proteins
  • Oxidoreductases
  • alternative oxidase