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Bifunctional role of the bc1 complex in plants. Mitochondrial bc1 complex catalyses both electron transport and
E Glaser1, A Eriksson, S Sjöling
1Department of Biochemistry, Arrhenius Laboratories for Natural Sciences, Stockholm University, Sweden.
FEBS Letters
|June 6, 1994
Abstract:
Nuclear encoded mitochondrial precursor proteins are cleaved to mature size products by the general mitochondrial processing peptidase (MPP). In contrast to non-plant sources where MPP is a matrix enzyme, the plant mitochondrial MPP is localised in the inner membrane and constitutes an integral part of the bc1 complex of the respiratory chain. Core proteins of the complex are immunologically related and show high sequence similarity to the MPP subunits from non-plant sources. The bc1 complex in plants is thus bifunctional, being involved both in respiration and in protein processing.