RIP1/YEL024W Literature Guide Help

Other names published for RIP1: ubiquinol--cytochrome-c reductase catalytic subunit RIP1, YEL024W

RIP1 - Protein Physical Properties (33)

Results: 1 - 30 of 33 records
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ReferenceOther 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
Covian R and Trumpower BL  (2009) The Rate-limiting Step in the Cytochrome bc1 Complex (Ubiquinol-Cytochrome c Oxidoreductase) Is Not Changed by Inhibition of Cytochrome b-dependent Deprotonation: IMPLICATIONS FOR THE MECHANISM OF UBIQUINOL OXIDATION AT CENTER P OF THE bc1 COMPLEX. J Biol Chem 284(21):14359-67
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
Covian R and Trumpower BL  (2006) Regulatory interactions between ubiquinol oxidation and ubiquinone reduction sites in the dimeric cytochrome bc1 complex. J Biol Chem 281(41):30925-32
Fisher N, et al.  (2004) Disruption of the interaction between the Rieske iron-sulfur protein and cytochrome b in the yeast bc1 complex owing to a human disease-associated mutation within cytochrome b. Eur J Biochem 271(7):1292-8
Fisher N, et al.  (2004) Human disease-related mutations in cytochrome b studied in yeast. J Biol Chem 279(13):12951-8
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
Denke E, et al.  (1998) Alteration of the midpoint potential and catalytic activity of the rieske iron-sulfur protein by changes of amino acids forming hydrogen bonds to the iron-sulfur cluster. J Biol Chem 273(15):9085-93
Obungu VH, et al.  (1998) The role of charged amino acids in the alpha1-beta4 loop of the iron-sulfur protein of the cytochrome bc1 complex of yeast mitochondria. J Biol Chem 273(19):11917-22
Brandt U, et al.  (1994) Isolation and characterization of QCR10, the nuclear gene encoding the 8.5-kDa subunit 10 of the Saccharomyces cerevisiae cytochrome bc1 complex. J Biol Chem 269(17):12947-53
Geier BM, et al.  (1992) Point mutation in cytochrome b of yeast ubihydroquinone:cytochrome-c oxidoreductase causing myxothiazol resistance and facilitated dissociation of the iron-sulfur subunit. Eur J Biochem 208(2):375-80
Nobrega FG, et al.  (1992) BCS1, a novel gene required for the expression of functional Rieske iron-sulfur protein in Saccharomyces cerevisiae. EMBO J 11(11):3821-9
Wu M and Tzagoloff A  (1989) Identification and characterization of a new gene (CBP3) required for the expression of yeast coenzyme QH2-cytochrome c reductase. J Biol Chem 264(19):11122-30
Beckmann JD, et al.  (1987) Isolation and characterization of the nuclear gene encoding the Rieske iron-sulfur protein (RIP1) from Saccharomyces cerevisiae. J Biol Chem 262(18):8901-9
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
Results: 1 - 30 of 33 records
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