Details
| Original language | English |
|---|---|
| Pages (from-to) | 423-436 |
| Number of pages | 14 |
| Journal | Journal of Bioenergetics and Biomembranes |
| Volume | 27 |
| Issue number | 4 |
| Publication status | Published - Aug 1995 |
| Externally published | Yes |
Abstract
Cytochrome c reductase from potato has been extensively studied with respect to its catalytic activities, its subunit composition, and the biogenesis of individual subunits. Molecular characterization of all 10 subunits revealed that the high-molecular-weight subunits exhibit striking homologies with the components of the general mitochondrial processing peptidase (MPP) from fungi and mammals. Some of the other subunits show differences in the structure of their targeting signals or in their molecular composition when compared to their counterparts from heterotrophic organisms. The proteolytic activity of MPP was found in the cytochrome c reductase complexes from potato, spinach, and wheat, suggesting that the integration of the protease into this respiratory complex is a general feature of higher plants.
Keywords
- bc complex, Cytochrome c reductase, mitochondria, mitochondrial processing peptidase, protein import, respiratory chain
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Physiology
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: Journal of Bioenergetics and Biomembranes, Vol. 27, No. 4, 08.1995, p. 423-436.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The bifunctional cytochrome c reductase/processing peptidase complex from plant mitochondria
AU - Braun, Hans-Peter
AU - Schmitz, Udo
PY - 1995/8
Y1 - 1995/8
N2 - Cytochrome c reductase from potato has been extensively studied with respect to its catalytic activities, its subunit composition, and the biogenesis of individual subunits. Molecular characterization of all 10 subunits revealed that the high-molecular-weight subunits exhibit striking homologies with the components of the general mitochondrial processing peptidase (MPP) from fungi and mammals. Some of the other subunits show differences in the structure of their targeting signals or in their molecular composition when compared to their counterparts from heterotrophic organisms. The proteolytic activity of MPP was found in the cytochrome c reductase complexes from potato, spinach, and wheat, suggesting that the integration of the protease into this respiratory complex is a general feature of higher plants.
AB - Cytochrome c reductase from potato has been extensively studied with respect to its catalytic activities, its subunit composition, and the biogenesis of individual subunits. Molecular characterization of all 10 subunits revealed that the high-molecular-weight subunits exhibit striking homologies with the components of the general mitochondrial processing peptidase (MPP) from fungi and mammals. Some of the other subunits show differences in the structure of their targeting signals or in their molecular composition when compared to their counterparts from heterotrophic organisms. The proteolytic activity of MPP was found in the cytochrome c reductase complexes from potato, spinach, and wheat, suggesting that the integration of the protease into this respiratory complex is a general feature of higher plants.
KW - bc complex
KW - Cytochrome c reductase
KW - mitochondria
KW - mitochondrial processing peptidase
KW - protein import
KW - respiratory chain
UR - http://www.scopus.com/inward/record.url?scp=0028857080&partnerID=8YFLogxK
U2 - 10.1007/BF02110005
DO - 10.1007/BF02110005
M3 - Article
C2 - 8595978
AN - SCOPUS:0028857080
VL - 27
SP - 423
EP - 436
JO - Journal of Bioenergetics and Biomembranes
JF - Journal of Bioenergetics and Biomembranes
SN - 0145-479X
IS - 4
ER -