PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2977133-0 1988 Oxygen exchange during the acto-subfragment-1 ATPase reaction: evidence for the two-route mechanism of the actomyosin ATPase reaction. Oxygen 0-6 dynein axonemal heavy chain 8 Homo sapiens 46-52 10924349-2 2000 We demonstrate that in vitro the Na(+)/K(+)-ATPase, a non heme-protein, is able to disproportionate H(2)O(2) catalatically into dioxygen and water, as well as C(40) catalase. Oxygen 128-136 dynein axonemal heavy chain 8 Homo sapiens 44-50 8415909-4 1993 Among the different quenchers tested, oxygen quenching alone was sensitive to calcium binding to the ATPase, indicating that oxygen quenched tryptophan residues located in regions of the ATPase molecule which undergo conformational changes upon calcium binding. Oxygen 38-44 dynein axonemal heavy chain 8 Homo sapiens 101-107 8415909-4 1993 Among the different quenchers tested, oxygen quenching alone was sensitive to calcium binding to the ATPase, indicating that oxygen quenched tryptophan residues located in regions of the ATPase molecule which undergo conformational changes upon calcium binding. Oxygen 38-44 dynein axonemal heavy chain 8 Homo sapiens 187-193 8415909-4 1993 Among the different quenchers tested, oxygen quenching alone was sensitive to calcium binding to the ATPase, indicating that oxygen quenched tryptophan residues located in regions of the ATPase molecule which undergo conformational changes upon calcium binding. Oxygen 125-131 dynein axonemal heavy chain 8 Homo sapiens 101-107 8415909-4 1993 Among the different quenchers tested, oxygen quenching alone was sensitive to calcium binding to the ATPase, indicating that oxygen quenched tryptophan residues located in regions of the ATPase molecule which undergo conformational changes upon calcium binding. Oxygen 125-131 dynein axonemal heavy chain 8 Homo sapiens 187-193 1831462-0 1991 Kinetics of ATP release and Pi binding during the ATPase cycle of lethocerus flight muscle fibres, using phosphate-water oxygen exchange. Oxygen 121-127 dynein axonemal heavy chain 8 Homo sapiens 50-56 1831462-1 1991 Rate constants have been obtained using oxygen isotope exchange techniques for steps controlling ATP release and Pi binding in the ATPase cycle of insect flight muscle fibres from the giant waterbug Lethecerus. Oxygen 40-46 dynein axonemal heavy chain 8 Homo sapiens 131-137 2977133-0 1988 Oxygen exchange during the acto-subfragment-1 ATPase reaction: evidence for the two-route mechanism of the actomyosin ATPase reaction. Oxygen 0-6 dynein axonemal heavy chain 8 Homo sapiens 118-124 2977133-1 1988 The oxygen exchange occurring during the acto-S-1 ATPase reaction was analyzed based on the distribution of 18O-labeled species of P1 using [gamma-18O]ATP as a substrate. Oxygen 4-10 dynein axonemal heavy chain 8 Homo sapiens 50-56 6309819-2 1983 Likewise, during net ATP hydrolysis by the Mg2+-activated chloroplast ATPase, the extent of water oxygen incorporation into each Pi released increases as the ATP, GTP, or ITP concentration is decreased. Oxygen 98-104 dynein axonemal heavy chain 8 Homo sapiens 70-76 6309819-6 1983 Activation of the chloroplast ATPase by either heat or trypsin results in similar catalytic behavior as monitored by ATP modulation of oxygen exchanges during hydrolysis in the presence of Mg2+. Oxygen 135-141 dynein axonemal heavy chain 8 Homo sapiens 30-36 29032642-3 2017 The light-dependent ATPase activity of CMV was lowered in the presence of O2, but the activity increased to the level observed under anaerobic condition when the reaction mixture was supplemented with ascorbic acid (>=0.5 mM). Oxygen 74-76 dynein axonemal heavy chain 8 Homo sapiens 20-26 6216920-0 1982 [Localization of the ATPase site of nitrogenase by isotopic oxygen exchange [180]-Pi in equilibrium with H20]. Oxygen 60-66 dynein axonemal heavy chain 8 Homo sapiens 21-27 4241910-6 1969 Apparently an ATPase is activated by depolarization; the resulting ADP is probably the trigger for the increase in oxygen uptake.3. Oxygen 115-121 dynein axonemal heavy chain 8 Homo sapiens 14-20 4239123-0 1969 ATPase content of striated muscle stressed in O2-CO2 and hyperbaric N2-O2-CO2 atmospheres. Oxygen 46-48 dynein axonemal heavy chain 8 Homo sapiens 0-6 4239123-0 1969 ATPase content of striated muscle stressed in O2-CO2 and hyperbaric N2-O2-CO2 atmospheres. Oxygen 50-52 dynein axonemal heavy chain 8 Homo sapiens 0-6 153910-1 1979 The capacity of various ATPase preparations from beef heart mitochondria to catalyze exchange of phosphate oxygens with water has been evaluated. Oxygen 107-114 dynein axonemal heavy chain 8 Homo sapiens 24-30 670189-7 1978 Presence of this component, which is likely a contaminating ATPase, provides a simple explanation of the apparent nonequivalence of phosphate oxygens which has been observed. Oxygen 142-149 dynein axonemal heavy chain 8 Homo sapiens 60-66 26615669-5 2016 Under light illumination, PSII can split water into protons, oxygen, and electrons and can generate a proton gradient for ATPase to produce ATP. Oxygen 61-67 dynein axonemal heavy chain 8 Homo sapiens 122-128