PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19348906-1 2009 Cytochrome b is a pivotal protein subunit of the cytochrome bc(1) complex and forms the ubiquinol oxidation site in the enzyme that is generally thought to be the primary site where electrons are aberrantly diverted from the enzyme, reacting with oxygen to form superoxide anion. ubiquinol 88-97 cytochrome b Saccharomyces cerevisiae S288C 0-12 19325183-0 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. ubiquinol 197-206 cytochrome b Saccharomyces cerevisiae S288C 30-42 12767232-8 2003 Together with the X-ray structures, these results suggest substrate ubiquinol binds in a fashion similar to that of stigmatellin with H-bonds between H161 of the Rieske iron-sulfur protein and E272 of the cyt b protein. ubiquinol 68-77 cytochrome b Saccharomyces cerevisiae S288C 205-210 17145759-0 2007 Mutational analysis of cytochrome b at the ubiquinol oxidation site of yeast complex III. ubiquinol 43-52 cytochrome b Saccharomyces cerevisiae S288C 23-35 15718226-0 2005 Cytochrome b mutations that modify the ubiquinol-binding pocket of the cytochrome bc1 complex and confer anti-malarial drug resistance in Saccharomyces cerevisiae. ubiquinol 39-48 cytochrome b Saccharomyces cerevisiae S288C 0-12 17383607-1 2007 Hydroxy-naphthoquinones are competitive inhibitors of the cytochrome bc(1) complex that bind to the ubiquinol oxidation site between cytochrome b and the iron-sulfur protein and presumably mimic a transition state in the ubiquinol oxidation reaction catalyzed by the enzyme. ubiquinol 100-109 cytochrome b Saccharomyces cerevisiae S288C 58-70 17383607-1 2007 Hydroxy-naphthoquinones are competitive inhibitors of the cytochrome bc(1) complex that bind to the ubiquinol oxidation site between cytochrome b and the iron-sulfur protein and presumably mimic a transition state in the ubiquinol oxidation reaction catalyzed by the enzyme. ubiquinol 221-230 cytochrome b Saccharomyces cerevisiae S288C 58-70 15833742-5 2005 We propose that electron transfer between cytochrome b subunits minimizes the formation of semiquinone-ferrocytochrome b(H) complexes at center N and favors ubiquinol oxidation at center P by increasing the amount of oxidized cytochrome b. ubiquinol 157-166 cytochrome b Saccharomyces cerevisiae S288C 42-54 9932648-0 1998 Exogenous ubiquinol analogues affect the fluorescence of NCD-4 bound to aspartate-160 of yeast cytochrome b. ubiquinol 10-19 cytochrome b Saccharomyces cerevisiae S288C 95-107 10531315-4 1999 With cytochrome bc(1) complex from a yeast mutant that cannot synthesize ubiquinone, cytochrome b reduction by either menaquinol or ubiquinol was rapid and monophasic. ubiquinol 132-141 cytochrome b Saccharomyces cerevisiae S288C 5-17 2078867-4 1990 Their ubiquinol (QH2)-cytochrome c reductase/mole cytochrome b activity decreased by about 50%. ubiquinol 6-15 cytochrome b Saccharomyces cerevisiae S288C 50-62 9201979-3 1997 Pre-steady-state kinetics indicate that these compounds bind to the complex on the intermembrane space side, thereby blocking reduction of cytochrome b via the ubiquinol oxidation site. ubiquinol 160-169 cytochrome b Saccharomyces cerevisiae S288C 139-151 8394320-1 1993 The iron-sulfur protein of the cytochrome bc1 complex oxidizes ubiquinol at center P in the protonmotive Q cycle mechanism, transferring one electron to cytochrome c1 and generating a low-potential ubisemiquinone anion which reduces the low-potential cytochrome b-566 heme group. ubiquinol 63-72 cytochrome b Saccharomyces cerevisiae S288C 31-43 1651245-6 1991 This study provides biochemical and biophysical information for identifying a region in mitochondrial cytochrome b that may fulfill a crucial role in the binding of ubiquinol to the bc1 complex. ubiquinol 165-174 cytochrome b Saccharomyces cerevisiae S288C 102-114 9587406-0 1998 Dicyclohexylcarbodiimide inhibits proton pumping in ubiquinol:cytochrome c oxidoreductase of Rhodobacter sphaeroides and binds to aspartate-187 of cytochrome b. ubiquinol 52-61 cytochrome b Saccharomyces cerevisiae S288C 147-159 7673215-0 1995 Role of the evolutionarily conserved cytochrome b tryptophan 142 in the ubiquinol oxidation catalyzed by the bc1 complex in the yeast Saccharomyces cerevisiae. ubiquinol 72-81 cytochrome b Saccharomyces cerevisiae S288C 37-49 8200339-0 1994 Analysis of cytochrome-b amino acid residues forming the contact face with the iron-sulfur subunit of ubiquinol:cytochrome-c reductase in Saccharomyces cerevisiae. ubiquinol 102-111 cytochrome b Saccharomyces cerevisiae S288C 12-24 2078867-4 1990 Their ubiquinol (QH2)-cytochrome c reductase/mole cytochrome b activity decreased by about 50%. ubiquinol 17-20 cytochrome b Saccharomyces cerevisiae S288C 50-62 2154475-7 1990 We report here nine novel cytochrome b structures conferring a variety of respiratory sufficient phenotypes, obtained from five respiratory deficient mutations affecting a short region of the protein (positions 131-138 of the polypeptide chain), presumably belonging to the ubiquinol oxidizing center of the bc1 complex. ubiquinol 274-283 cytochrome b Saccharomyces cerevisiae S288C 26-38 2543567-1 1989 Inactivation of the gene encoding the 11-kDa subunit VIII of yeast ubiquinol:cytochrome c oxidoreductase leads to an inactive complex, which lacks detectable cytochrome b [Maarse, A. C., De Haan, M., Schoppink, P. J., Berden, J. ubiquinol 67-76 cytochrome b Saccharomyces cerevisiae S288C 158-170