PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19325183-6 2009 The rate and E(a) of the slow reaction of quinol with oxygen that are observed after cytochrome b is reduced were unaffected by the E272Q substitution, whereas the Y185F mutation modified only its rate. Oxygen 54-60 cytochrome b Saccharomyces cerevisiae S288C 85-97 19478336-5 2009 The rate of superoxide generation by the reconstituted bc(1) complex increased exponentially with increased magnitude of the membrane potential, a finding that is compatible with the suggestion that membrane potential inhibits electron transfer from the cytochrome b(L) to b(H) hemes, thereby promoting the formation of a ubisemiquinone radical that interacts with oxygen to generate superoxide. Oxygen 365-371 cytochrome b Saccharomyces cerevisiae S288C 254-266 20171157-2 2010 The Cytb(558) is the catalytic core of the NADPH-oxidase that generates a superoxide anion from oxygen by using a reducing equivalent provided by NADPH via FAD and two hemes. Oxygen 96-102 cytochrome b Saccharomyces cerevisiae S288C 4-8 6274398-2 1981 The doses required for 50% inhibition were 0.58 mol myxothiazol/mol cytochrome b for oxygen consumption of beef heart mitochondria, and 0.45 mol/mol cytochrome b for NADH oxidation by submitochondrial particles. Oxygen 85-91 cytochrome b Saccharomyces cerevisiae S288C 68-80 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. Oxygen 247-253 cytochrome b Saccharomyces cerevisiae S288C 0-12 19348906-2 2009 In addition, recent studies have shown that mutations in cytochrome b can substantially increase rates of oxygen radical formation by the bc(1) complex. Oxygen 106-112 cytochrome b Saccharomyces cerevisiae S288C 57-69 19348906-3 2009 It would, thus, be advantageous to be able to manipulate cytochrome b by mutagenesis of the cytochrome b gene to better understand the role of cytochrome b in oxygen radical formation. Oxygen 159-165 cytochrome b Saccharomyces cerevisiae S288C 57-69 19348906-3 2009 It would, thus, be advantageous to be able to manipulate cytochrome b by mutagenesis of the cytochrome b gene to better understand the role of cytochrome b in oxygen radical formation. Oxygen 159-165 cytochrome b Saccharomyces cerevisiae S288C 92-104 19348906-3 2009 It would, thus, be advantageous to be able to manipulate cytochrome b by mutagenesis of the cytochrome b gene to better understand the role of cytochrome b in oxygen radical formation. Oxygen 159-165 cytochrome b Saccharomyces cerevisiae S288C 92-104 235982-17 1975 The kinetics of redox changes in cytochrome b, in the presence of antimycin and oxygen, are distinctly different in the mutant and wild-type particles. Oxygen 80-86 cytochrome b Saccharomyces cerevisiae S288C 33-45 235982-18 1975 They indicate that ubiquinone plays an important role in the phenomenon of the increased reducibility of cytochrome b induced by antimycin plus oxygen. Oxygen 144-150 cytochrome b Saccharomyces cerevisiae S288C 105-117