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Plant respiratory chain branches at the level of ubiquinone from where the elec­trons flow through the cytochrome pathway or to alternative oxidase. Transfer of electrons from ubiquinone to oxygen by alternative oxidase has a non-protonmotive character and, by bypassing two sites of H pumping in complexes III and IV, lowers the energy efficiency of respiration. In this paper we review theoretical and experi­mental studies about the structure and possible function of alternative oxidase. The evidence for specific gene expression dependent on the physiological, developmental and environmental conditions is also described. We underline the physiological role of alternative oxidase as a "survival" protein that allows plants to cope with the stressful environment.
Uncoupling proteins, members of the mitochondrial carrier family, are present in mito­chondrial inner membrane and mediate free fatty acid-activated, purine-nucleo- tide-inhibited H+ re-uptake. Since 1995, it has been shown that the uncoupling protein is present in many higher plants and some microorganisms like non-photosynthetic amoeboid protozoon, Acanthamoeba castellanii and non-fermentative yeast Candida parapsilosis. In mitochondria of these organisms, uncoupling protein activity is revealed not only by stimulation of state 4 respiration by free fatty acids accompanied by decrease in membrane potential (these effects being partially released by ATP and GTP) but mainly by lowering ADP/O ratio during state 3 respiration. Plant and microorganism uncoupling proteins are able to divert very efficiently energy from oxidative phosphorylation, compet­ing for ΔμH+ with ATP synthase. Functional connection and physiological role of uncou­pling protein and alternative oxidase, two main energy-dissipating systems in plant-type mitochondria, are discussed.
Mitochondria of amoeba Acanthamoeba castellanii in addition to the conventional cytochrome pathway possess, like plant mitochondria, a cyanide-resistant alternative quinol oxidase. In mitochondria isolated from amoeba batch culture grown tempo­rarily at low temperature (6°C), higher respiration was accompanied by lower cou­pling parameters as compared to control culture (grown at 28°C). In the presence of benzohydroxamate, respiratory rates and coupling parameters were similar in both types of mitochondria indicating that growth in cold conditions did not disturb the cytochrome pathway. Increased contribution of alternative oxidase in total mitochon­drial respiration in low-temperature-grown amoeba cells was confirmed by calcula­tion of its contribution using ADP/O measurements. Furthermore, in mitochondria from low-temperature- grown cells the content of the alternative oxidase was in­creased and correlated with the increase in the unstimulated and GMP-stimulated cya­nide-resistant respiratory activity. A possible physiological role of higher activity of alternative oxidase as response to growth at a low temperature in unicellular organ­isms, such as amoeba, is discussed.
Lead, similar to other heavy metals and abiotic factors, causes many unfavorable changes at the subcellular and molecular levels in plant cells. An increased level of superoxide anion in Pisum sativum root cells treated with 1 mM Pb(NO3)2 evidenced oxidative stress conditions. We found increased activities of enzymatic components of the antioxidative system (catalase and superoxide dismutase) in the cytosol, mito- chondrial and peroxisomal fractions isolated from root cells of Pisum sativum grown in modified Hoagland medium in the presence of lead ions (0.5 or 1 mM). Two isoenzyme forms of superoxide dismutase (Cu,Zn-SOD and Mn-SOD) found in differ­ent subcellular compartments of pea roots were more active in Pb-treated plants than in control. Increased amount of alternative oxidase accompanied by an increased ac­tivity of this enzyme was found in mitochondria isolated from lead-treated roots. These results show that plants storing excessive amounts of lead in roots defend them­selves against the harmful oxidative stress caused by this heavy metal.
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