alternative oxidase

Alternative oxidase and uncoupling proteins similar to those found in mammals enable the process, which is still poorly understood.

This major metabolic difference between the parasite and its human host has made the T. brucei alternative oxidase an attractive target for drug design.

This metabolic pathway leading to the alternative oxidase diverges from the cytochrome-linked electron transport chain at the ubiquinone pool.

Plastid terminal oxidase and alternative oxidase are thought to have originated from a common ancestral di-iron carboxylate protein.

In fungi, the ability of the alternative oxidase to bypass inhibition of parts of the electron transport chain can contribute to fungicide resistance.

Another example of a divergent electron transport chain is the alternative oxidase, which is found in plants, as well as some fungi, protists, and possibly some animals.

The predicted structure is similar to that of the alternative oxidase, with an additional Exon 8 domain that is required for the plastid oxidase's activity and stability.

The plastid oxidase first evolved in ancient cyanobacteria and the alternative oxidase in proteobacteria before eukaryotic evolution and endosymbiosis events.

ESTs confirm the presence of complexes I and II, and indicate that this partial electron transport chain may lead to an alternative oxidase.

The enzyme was hypothesized to exist as a photosynthetic oxidase in 1982 and was verified by sequence similarity to the mitochondrial alternative oxidase (AOX).

This enzyme was first identified as a distinct oxidase pathway from cytochrome c oxidase as the alternative oxidase is resistant to inhibition by the poison cyanide.

However, the alternative oxidase is produced in response to stresses such as cold, reactive oxygen species, and infection by pathogens, as well as other factors that inhibit the full electron transport chain.

It is thought to involve a proton pumping respiratory dehydrogenase (the Ndh complex), and Immutans, an oxidase similar to the mitochondrial alternative oxidase, which reduces the plastoquinone pool.

Unusually, the bloodstream form of the protozoan parasite Trypanosoma brucei, which is the cause of sleeping sickness, depends entirely on the alternative oxidase pathway for cellular respiration through its electron transport chain.

The electron spin resonance study of Arabidopsis thaliana alternative oxidase AOX1a showed that the enzyme contains a hydroxo-bridged mixed-valent Fe(II)/Fe(III) binuclear iron center.

The alternative oxidase (AOX) is an enzyme that forms part of the electron transport chain in mitochondria of different organisms Proteins homologous to the mitochondrial oxidase have also been identified in bacterial genomes.

The expression of the alternative oxidase gene AOX is influenced by stresses such as cold, reactive oxygen species and infection by pathogens, as well as other factors that reduce electron flow through the cytochrome pathway of respiration.

In plants, some fungi and some protists with the alternative oxidase (AOX) enzyme in the mitochondrial electron transport chain system, salicylhdroxamic acid acts as an inhibitor of the enzyme, blocking the largely uninhibited flow of electrons through AOX.