Other names published for QCR8: COR5, ubiquinol--cytochrome-c reductase subunit 8, YJL166W
QCR8 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
QCR8 - Protein Physical Properties (25)
| Reference | Other Genes Addressed |
|---|---|
| Hasan SS, et al. (2011) Conservation of lipid functions in cytochrome bc complexes. J Mol Biol 414(1):145-62 | |
| Gonzalez-Cabo P, et al. (2010) Flavin adenine dinucleotide rescues the phenotype of frataxin deficiency. PLoS One 5(1):e8872 | |
| Cape JL, et al. (2009) Substrate redox potential controls superoxide production kinetics in the cytochrome bc complex. Biochemistry 48(45):10716-23 | |
| Hielscher R, et al. (2009) Monitoring the redox and protonation dependent contributions of cardiolipin in electrochemically induced FTIR difference spectra of the cytochrome bc(1) complex from yeast. Biochim Biophys Acta 1787(6):617-25 | |
| Rottenberg H, et al. (2009) Membrane Potential Greatly Enhances Superoxide Generation by the Cytochrome bc1 Complex Reconstituted into Phospholipid Vesicles. J Biol Chem 284(29):19203-10 | |
| Covian R and Trumpower BL (2008) The dimeric structure of the cytochrome bc(1) complex prevents center P inhibition by reverse reactions at center N. Biochim Biophys Acta 1777(7-8):1044-52 | |
| Covian R, et al. (2007) Asymmetric and redox-specific binding of quinone and quinol at center N of the dimeric yeast cytochrome bc1 complex. Consequences for semiquinone stabilization. J Biol Chem 282(33):24198-208 | |
| Ebert CE, et al. (2003) Aspartate-186 in the head group of the yeast iron-sulfur protein of the cytochrome bc1 complex contributes to the protein conformation required for efficient electron transfer. Biochim Biophys Acta 1607(2-3):65-78 | |
| Engstrom G, et al. (2003) Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complex. Biochemistry 42(10):2816-24 | |
| Sun J and Trumpower BL (2003) Superoxide anion generation by the cytochrome bc1 complex. Arch Biochem Biophys 419(2):198-206 | |
| Muller F, et al. (2002) Multiple Q-cycle bypass reactions at the Qo site of the cytochrome bc1 complex. Biochemistry 41(25):7866-74 | |
| Trumpower BL (2002) A concerted, alternating sites mechanism of ubiquinol oxidation by the dimeric cytochrome bc(1) complex. Biochim Biophys Acta 1555(1-3):166-73 | |
| Brasseur G, et al. (2001) Analysis of suppressor mutation reveals long distance interactions in the bc(1) complex of Saccharomyces cerevisiae. Biochim Biophys Acta 1506(2):89-102 | |
| Ghosh M, et al. (2001) Substituting leucine for alanine-86 in the tether region of the iron-sulfur protein of the cytochrome bc1 complex affects the mobility of the [2Fe2S] domain. Biochemistry 40(2):327-35 | |
| Schagger H and Pfeiffer K (2000) Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J 19(8):1777-83 | |
| Snyder CH and Trumpower BL (1999) Ubiquinone at center N is responsible for triphasic reduction of cytochrome b in the cytochrome bc(1) complex. J Biol Chem 274(44):31209-16 | |
| Boumans H, et al. (1997) The role of subunit VIII in the structural stability of the bc1 complex from Saccharomyces cerevisiae studied using hybrid complexes. Eur J Biochem 249(3):762-9 | |
| De Winde JH and Grivell LA (1995) Regulation of mitochondrial biogenesis in Saccharomyces cerevisiae. Intricate interplay between general and specific transcription factors in the promoter of the QCR8 gene. Eur J Biochem 233(1):200-8 | |
| Hemrika W, et al. (1993) A region of the C-terminal part of the 11-kDa subunit of ubiquinol-cytochrome-c oxidoreductase of the yeast Saccharomyces cerevisiae contributes to the structure of the Qout reaction domain. Eur J Biochem 215(3):601-9 | |
| Hemrika W and Berden JA (1990) Membrane topography of the subunits of ubiquinol-cytochrome-c oxidoreductase of Saccharomyces cerevisiae. The 14-kDa and the 11-kDa subunits face opposite sides of the mitochondrial inner membrane. Eur J Biochem 192(3):761-5 | |
| Kauten R, et al. (1987) The kinetics of reduction of yeast complex III by a substrate analog. J Biol Chem 262(18):8658-67 | |
| Tsai AL, et al. (1987) The kinetics of reoxidation of yeast complex III. An evaluation of the Q-cycle. J Biol Chem 262(18):8677-84 | |
| Beattie DS, et al. (1984) The preferential binding of dicyclohexylcarbodiimide to cytochrome b and phospholipids in soluble complex III from yeast mitochondria. J Biol Chem 259(16):10526-32 | |
| Sidhu A and Beattie DS (1982) Purification and polypeptide characterization of complex III from yeast mitochondria. J Biol Chem 257(13):7879-86 | |
| Tzagoloff A (1969) Assembly of the mitochondrial membrane system. I. Characterization of some enzymes of the inner membrane of yeast mitochondria. J Biol Chem 244(18):5020-6 |



