scholarly journals S15.13 Is cytochrome b glutamic acid 272 a quinol binding residue in the bc1 complex?

2008 ◽  
Vol 1777 ◽  
pp. S105
Author(s):  
Nadir Seddiki ◽  
Brigitte Meunier ◽  
Danielle Lemesle-Meunier ◽  
Carola Hunte ◽  
Gaël Brasseur
Keyword(s):  
Glutamic Acid ◽  
Cytochrome B ◽  
Bc1 Complex ◽  
Binding Residue ◽  
Quinol Binding

Characterization of mutations in the cytochrome b subunit of the bc1 complex of Rhodobacter sphaeroides that affect the quinone reductase site (Qc)

Biochemistry ◽  
1993 ◽  
Vol 32 (16) ◽  
pp. 4403-4410 ◽  
Author(s):  
Beth Hacker ◽  
Blanca Barquera ◽  
Antony R. Crofts ◽  
Robert B. Gennis
Keyword(s):  
Cytochrome B ◽  
Rhodobacter Sphaeroides ◽  
Quinone Reductase ◽  
Bc1 Complex ◽  
B Subunit

Tyrosine 147 of cytochrome b is required for efficient electron transfer at the ubihydroquinone oxidase site (Qo) of the cytochrome bc1 complex

Biochemistry ◽  
1995 ◽  
Vol 34 (49) ◽  
pp. 16004-16012 ◽  
Author(s):  
A. Sami Saribas ◽  
Huangen Ding ◽  
P. Leslie Dutton ◽  
Fevzi Daldal
Keyword(s):  
Electron Transfer ◽  
Cytochrome B ◽  
Cytochrome Bc1 ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex

scholarly journals Cbp3–Cbp6 interacts with the yeast mitochondrial ribosomal tunnel exit and promotes cytochrome b synthesis and assembly

2011 ◽  
Vol 193 (6) ◽  
pp. 1101-1114 ◽  
Author(s):  
Steffi Gruschke ◽  
Kirsten Kehrein ◽  
Katharina Römpler ◽  
Kerstin Gröne ◽  
Lars Israel ◽  
...  
Keyword(s):  
Cytochrome B ◽  
Genetic System ◽  
The Other ◽  
Bc1 Complex ◽  
Mitochondrial Ribosomes ◽  
Ribosomal Tunnel ◽  
Assembly Factor ◽  
Assembly Intermediate ◽  
The One ◽  
Essential Subunit

Mitochondria contain their own genetic system to express a small number of hydrophobic polypeptides, including cytochrome b, an essential subunit of the bc1 complex of the respiratory chain. In this paper, we show in yeast that Cbp3, a bc1 complex assembly factor, and Cbp6, a regulator of cytochrome b translation, form a complex that associates with the polypeptide tunnel exit of mitochondrial ribosomes and that exhibits two important functions in the biogenesis of cytochrome b. On the one hand, the interaction of Cbp3 and Cbp6 with mitochondrial ribosomes is necessary for efficient translation of cytochrome b transcript. On the other hand, the Cbp3–Cbp6 complex interacts directly with newly synthesized cytochrome b in an assembly intermediate that is not ribosome bound and that contains the assembly factor Cbp4. Our results suggest that synthesis of cytochrome b occurs preferentially on those ribosomes that have the Cbp3–Cbp6 complex bound to their tunnel exit, an arrangement that may ensure tight coordination of cytochrome b synthesis and assembly.

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