Functioning of a CSP310 stress protein is related to the shunting of electron transfer along the respiratory chain of winter wheat mitochondria

Autor:	Victor K. Voinikov, A. V. Kolesnichenko, O. I. Grabel’nykh, Tamara P. Pobezhimova
Rok vydání:	2006
Předmět:	Electron transfer Mitochondrial respiratory chain Biochemistry Coenzyme Q – cytochrome c reductase Respiratory chain food and beverages Phosphorylation Plant Science Biology Mitochondrion biology.organism_classification Electron transport chain Pisum
Zdroj:	Russian Journal of Plant Physiology. 53:332-339
ISSN:	1608-3407 1021-4437
DOI:	10.1134/s1021443706030071
Popis:	Using three-day-old winter-wheat (Triticum aestivum L.) and six-day-old pea (Pisum sativum L.) seedlings as examples, we studied the effects of inhibitors of the electron transfer chain of plant mitochondria on the uncoupling between oxidation and phosphorylation brought about by the CSP310 stress protein. This uncoupling was inhibited by cyanide and by antibodies against CSP310, but not inhibited by antimycin A. It was shown that, in plant mitochondria, the CSP310 stress protein is involved in the electron transfer via shunting the major cytochrome pathway. In this case, the electron transfer bypasses complex II, ubiquinone, and complex III of the mitochondrial respiratory chain and is realized in the following succession: complex I-CSP310-cytochrome c-complex IV. This electron-transfer pathway was found in winter grass mitochondria during the low-temperature stress and resulted in thermogenesis. It was concluded that CSP310 is a thermogenic system, which is activated in winter grass mitochondria during the low-temperature stress.
Databáze:	OpenAIRE
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