Abstract
A cytochrome bc1 complex, essentially free of bacteriochlorophyll, has been purified from the photosynthetic purple non-sulfur bacterium Rhodospirillum rubrum. The complex catalyzes electron flow from quinol to cytochrome c (turnover number = 75 s-1) that is inhibited by low concentrations of antimycin A and myxothiazol. The complex contains only three peptide subunits: cytochrome b (Mr = 35000); cytochrome c1 (Mr = 31000) and the Rieske iron-sulfur protein (Mr = 22400). Em values (pH 7.4) were measured for cytochrome c, (+ 320 mV) and the two hemes of cytochrome b (- 33 and -90 mV). Electron flow from quinol to cytochrome c is inhibited when the complex is pre-illuminated in the presence of a ubiquinone photoaffinity analog (azido-Q). During illumination, the azido-Q becomes covalently attached to the cytochrome b peptide and, to a lesser extent, to cytochrome c1.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 70-76 |
| Number of pages | 7 |
| Journal | BBA - Bioenergetics |
| Volume | 976 |
| Issue number | 1 |
| DOIs | |
| State | Published - 1989 |
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Keywords
- (R. rubrum)
- Cytochrome bc complex
- Electron transport chain
- Purple bacteria
- Quinone binding
ASJC Scopus subject areas
- Biophysics
- Medicine(all)
Cite this
The Rhodospirillum rubrum cytochrome bc1 complex : pep tide composition, prosthetic group content and quinone binding. / Kriauciunas, Aidas; Yu, Linda; Yu, Chang An; Wynn, R. Max; Knaff, David B.
In: BBA - Bioenergetics, Vol. 976, No. 1, 1989, p. 70-76.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The Rhodospirillum rubrum cytochrome bc1 complex
T2 - pep tide composition, prosthetic group content and quinone binding
AU - Kriauciunas, Aidas
AU - Yu, Linda
AU - Yu, Chang An
AU - Wynn, R. Max
AU - Knaff, David B.
PY - 1989
Y1 - 1989
N2 - A cytochrome bc1 complex, essentially free of bacteriochlorophyll, has been purified from the photosynthetic purple non-sulfur bacterium Rhodospirillum rubrum. The complex catalyzes electron flow from quinol to cytochrome c (turnover number = 75 s-1) that is inhibited by low concentrations of antimycin A and myxothiazol. The complex contains only three peptide subunits: cytochrome b (Mr = 35000); cytochrome c1 (Mr = 31000) and the Rieske iron-sulfur protein (Mr = 22400). Em values (pH 7.4) were measured for cytochrome c, (+ 320 mV) and the two hemes of cytochrome b (- 33 and -90 mV). Electron flow from quinol to cytochrome c is inhibited when the complex is pre-illuminated in the presence of a ubiquinone photoaffinity analog (azido-Q). During illumination, the azido-Q becomes covalently attached to the cytochrome b peptide and, to a lesser extent, to cytochrome c1.
AB - A cytochrome bc1 complex, essentially free of bacteriochlorophyll, has been purified from the photosynthetic purple non-sulfur bacterium Rhodospirillum rubrum. The complex catalyzes electron flow from quinol to cytochrome c (turnover number = 75 s-1) that is inhibited by low concentrations of antimycin A and myxothiazol. The complex contains only three peptide subunits: cytochrome b (Mr = 35000); cytochrome c1 (Mr = 31000) and the Rieske iron-sulfur protein (Mr = 22400). Em values (pH 7.4) were measured for cytochrome c, (+ 320 mV) and the two hemes of cytochrome b (- 33 and -90 mV). Electron flow from quinol to cytochrome c is inhibited when the complex is pre-illuminated in the presence of a ubiquinone photoaffinity analog (azido-Q). During illumination, the azido-Q becomes covalently attached to the cytochrome b peptide and, to a lesser extent, to cytochrome c1.
KW - (R. rubrum)
KW - Cytochrome bc complex
KW - Electron transport chain
KW - Purple bacteria
KW - Quinone binding
UR - http://www.scopus.com/inward/record.url?scp=0024972981&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0024972981&partnerID=8YFLogxK
U2 - 10.1016/S0005-2728(89)80190-2
DO - 10.1016/S0005-2728(89)80190-2
M3 - Article
C2 - 2548618
AN - SCOPUS:0024972981
VL - 976
SP - 70
EP - 76
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
SN - 0005-2728
IS - 1
ER -