scholarly journals Deletion of QCR6, the gene encoding subunit six of the mitochondrial cytochrome bc1 complex, blocks maturation of cytochrome c1, and causes temperature-sensitive petite growth in Saccharomyces cerevisiae.

1994 ◽  
Vol 269 (2) ◽  
pp. 1270-1275
Author(s):  
M. Yang ◽  
B.L. Trumpower
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cytochrome Bc1 ◽  
Temperature Sensitive ◽  
Mitochondrial Cytochrome ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex ◽  
Gene Encoding ◽  
Cytochrome C1

Assignment of the Gene for the Cytochrome c1 Subunit of the Mitochondrial Cytochrome bc1 Complex (CYC1) to Human Chromosome 8q24.3

Genomics ◽  
1994 ◽  
Vol 19 (2) ◽  
pp. 400-401 ◽  
Author(s):  
Alessandra M.V. Duncan ◽  
Takayuki Ozawa ◽  
Hiroshi Suzuki ◽  
Rima Rozen
Keyword(s):  
Human Chromosome ◽  
Cytochrome Bc1 ◽  
Mitochondrial Cytochrome ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex ◽  
Cytochrome C1

A novel electron transfer mechanism suggested by crystallographic studies of mitochondrial cytochrome bc1 complex

1998 ◽  
Vol 76 (5) ◽  
pp. 673-679 ◽  
Author(s):  
Di Xia ◽  
Hoeon Kim ◽  
Chang-An Yu ◽  
Linda Yu ◽  
Anatoly Kachurin ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Transmembrane Helix ◽  
Transfer Mechanism ◽  
Cytochrome Bc1 ◽  
Space Region ◽  
Mitochondrial Cytochrome ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex ◽  
Electron Transfer Mechanism ◽  
Cytochrome C1

The crystal structure of bovine mitochondrial cytochrome bc1 complex, an integral membrane protein complex of 11 different subunits with a total molecular mass of 242 kDa, demonstrated a tightly associated dimer consisting of three major regions: a matrix region primarily made of subunits core1, core2, 6, and 9; a transmembrane-helix region of 26 helices in the dimer contributed by cytochrome b, cytochrome c1, the Rieske iron-sulfur protein (ISP), subunits 7, 10, and 11; and an intermembrane-space region composed of extramembrane domains of ISP, cytochrome c1, and subunit 8. The structure also revealed the positions of and distances between irons of prosthetic groups, and two symmetry related cavities in the transmembrane-helix region upon dimerization of the bc1 complex. Extensive crystallographic studies on crystals of bc1 complexed with inhibitors of electron transfer identified binding pockets for both Qo and Qi site inhibitors. Discrete binding sites for subtypes of Qo site inhibitors have been mapped onto the Qo binding pocket, and bindings of different subtypes of Qo site inhibitors are capable of inducing dramatic conformational changes in the extramembrane domain of ISP. A novel electron transfer mechanism for the bc1 complex consistent with crystallographic observations is discussed.Key words: bc1 complex, electron transfer, structure, conformational change, inhibitor.

Resolution of the circular dichroism spectra of the mitochondrial cytochrome bc1 complex

1987 ◽  
Vol 892 (3) ◽  
pp. 245-252 ◽  
Author(s):  
Mauro Degli Esposti ◽  
Massimo Crimi ◽  
Christine M. Samworth ◽  
Giancarlo Solaini ◽  
Giorgio Lenaz
Keyword(s):  
Circular Dichroism ◽  
Cytochrome Bc1 ◽  
Mitochondrial Cytochrome ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex ◽  
Circular Dichroism Spectra ◽  
Circular Dichroïsm
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