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Bifunctional role of the bc 1 complex in plants Mitochondrial bc 1 complex catalyses both electron transport and protein processing
Author(s) -
Glaser Elzbieta,
Eriksson AnnaCarin,
Sjöling Sara
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00312-2
Subject(s) - mitochondrial matrix , bifunctional , mitochondrion , inner mitochondrial membrane , electron transport chain , respiratory chain , chemistry , biochemistry , phosphofructokinase 2 , biophysics , mitochondrial respiratory chain , inner membrane , biology , enzyme , cytosol , catalysis
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 bc 1 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 bc 1 complex in plants is thus bifunctional, being involved both in respiration and in protein processing.