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Updated: Aug 11, 2026

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
Published on: March 13, 2014
Non-phosphorylating bypass of the plant mitochondrial respiratory chain by stress protein CSP 310
A V Kolesnichenko1, O I Grabelnych, T P Pobezhimova
1Siberian Institute of Plant Physiology and Biochemistry, Russian Academy of Sciences, Irkutsk-33, P.O. Box 1243, 664033 Irkutsk, Russia. akol@sifibr.irk.ru
Abstract:
Recently, it has been reported that the cold-stress protein CSP 310, discovered in the cytoplasm of cold-resistant winter cereals, causes uncoupling of oxidative phosphorylation during cold stress. To understand how the uncoupling mechanism of CSP differs from that of cyanide-insensitive alternative oxidase and plant mitochondrial uncoupling protein, we determined the effect of respiratory-chain inhibition on winter wheat (Triticum aestivum L. cv. Zalarinka) mitochondria. Our data show a possible involvement of stress protein CSP 310 in mitochondrial electron transport in winter wheat. CSP 310 shunts electrons around the main cytochrome pathway of the mitochondrial respiratory chain, i.e. electron flow bypasses ubiquinone and complex III via CSP 310 to complex IV.
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