PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8914838-1 1996 Two mechanisms have been identified for the H2O2-dependent epoxidation of styrenes by sperm whale myoglobin (Mb) [S. Rao, A. Wilks, and P. R. Ortiz de Montellano, J. Biol. Hydrogen Peroxide 44-48 myoglobin Physeter catodon 98-107 7757198-0 1995 The role of H2O2-generated myoglobin radical in crosslinking of myosin. Hydrogen Peroxide 12-16 myoglobin Physeter catodon 27-36 7757198-1 1995 The mechanism of myoglobin/H2O2 derived peroxidation of myosin was studied by comparing the catalytic activity of myoglobin and horseradish peroxidase using O-dianisidine, N-acetyl tyrosine and myosin as substrates. Hydrogen Peroxide 27-31 myoglobin Physeter catodon 114-123 7757198-5 1995 Since the suicidal interaction of myoglobin with H2O2 forms unstable tyrosine radicals, we suggest that the increased activity of myoglobin on myosin results from an efficient electron transfer between surface tyrosines of myosin and myoglobin but not horseradish peroxidase. Hydrogen Peroxide 49-53 myoglobin Physeter catodon 34-43 7757198-5 1995 Since the suicidal interaction of myoglobin with H2O2 forms unstable tyrosine radicals, we suggest that the increased activity of myoglobin on myosin results from an efficient electron transfer between surface tyrosines of myosin and myoglobin but not horseradish peroxidase. Hydrogen Peroxide 49-53 myoglobin Physeter catodon 130-139 7757198-5 1995 Since the suicidal interaction of myoglobin with H2O2 forms unstable tyrosine radicals, we suggest that the increased activity of myoglobin on myosin results from an efficient electron transfer between surface tyrosines of myosin and myoglobin but not horseradish peroxidase. Hydrogen Peroxide 49-53 myoglobin Physeter catodon 130-139 8125933-7 1994 The stereochemical results, supported by 18O-labeling studies, definitively rule out a significant role for singlet oxygen in the myoglobin-catalyzed, H2O2-dependent oxidation of linoleic acid. Hydrogen Peroxide 151-155 myoglobin Physeter catodon 130-139 8125933-8 1994 The myoglobin protein radical formed with H2O2 also plays no part in the reaction because the Km and Vmax values for the oxidation of linoleic acid are similar for native myoglobin and two mutants (K102Q/Y103F/Y146F/Y151F and H64V/K102Q/Y103F/Y146F/Y151F) with no tyrosine residues. Hydrogen Peroxide 42-46 myoglobin Physeter catodon 4-13 1315742-0 1992 Intramolecular translocation of the protein radical formed in the reaction of recombinant sperm whale myoglobin with H2O2. Hydrogen Peroxide 117-121 myoglobin Physeter catodon 102-111 1398221-1 1992 The reactivity of the endogenous antioxidants ascorbate, ergothioneine, and urate toward the high oxidation state of sperm whale myoglobin, ferrylmyoglobin-formed upon oxidation of metmyoglobin by H2O2--was evaluated by optical spectroscopy and SDS-PAGE analysis. Hydrogen Peroxide 197-201 myoglobin Physeter catodon 129-138 3182873-1 1988 Coupling of Tyr-103 to Tyr-151 in the H2O2-mediated cross-linking of sperm whale myoglobin. Hydrogen Peroxide 38-42 myoglobin Physeter catodon 81-90 3182873-7 1988 Replacement of the prosthetic group of sperm whale myoglobin with zinc protoporphyrin IX prevents H2O2-induced dimerization even when intact horse metmyoglobin is present in the incubation. Hydrogen Peroxide 98-102 myoglobin Physeter catodon 51-60 12855712-0 2003 Intra- and intermolecular transfers of protein radicals in the reactions of sperm whale myoglobin with hydrogen peroxide. Hydrogen Peroxide 103-120 myoglobin Physeter catodon 88-97 25372675-1 2014 Sperm whale myoglobin (Mb) functions as an oxygen-storage protein, but in the ferric state it possesses a weak peroxidase activity which enables it to carry out H2O2-dependent dehalogenation reactions. Hydrogen Peroxide 161-165 myoglobin Physeter catodon 12-21 27521-6 1978 Kangaroo myoglobin(IV) may be prepared by reaction of ferrous myoglobin with hydrogen peroxide. Hydrogen Peroxide 77-94 myoglobin Physeter catodon 9-18 27521-6 1978 Kangaroo myoglobin(IV) may be prepared by reaction of ferrous myoglobin with hydrogen peroxide. Hydrogen Peroxide 77-94 myoglobin Physeter catodon 62-71 565653-1 1978 The compound formation between soybean leghemoglobins a and c and H2O2 or ethyl hydroperoxide has been studied and compared with the hydrogen peroxide compound of sperm whale myoglobin. Hydrogen Peroxide 133-150 myoglobin Physeter catodon 175-184 17173408-3 2006 Furthermore, it was found that the reconstituted myoglobin catalyzed the H2O2-dependent oxidations of substrates such as guaiacol, thioanisole, and styrene. Hydrogen Peroxide 73-77 myoglobin Physeter catodon 49-58 15749393-2 2005 The present study demonstrates that the sperm whale myoglobin tyrosyl radical, formed by hydrogen peroxide-dependent self-peroxidation, can either react with another tyrosyl radical, resulting in a dityrosine cross-linkage, or react with the spin trap DMPO to form a diamagnetic nitrone adduct. Hydrogen Peroxide 89-106 myoglobin Physeter catodon 52-61 15749393-3 2005 The reaction of sperm whale myoglobin with equimolar hydrogen peroxide resulted in the formation of a myoglobin dimer detectable by electrophoresis/protein staining. Hydrogen Peroxide 53-70 myoglobin Physeter catodon 28-37 15749393-3 2005 The reaction of sperm whale myoglobin with equimolar hydrogen peroxide resulted in the formation of a myoglobin dimer detectable by electrophoresis/protein staining. Hydrogen Peroxide 53-70 myoglobin Physeter catodon 102-111 9890961-0 1999 Reactions of sperm whale myoglobin with hydrogen peroxide. Hydrogen Peroxide 40-57 myoglobin Physeter catodon 25-34 9915818-0 1999 Effects of the location of distal histidine in the reaction of myoglobin with hydrogen peroxide. Hydrogen Peroxide 78-95 myoglobin Physeter catodon 63-72 9890961-9 1999 Combining the mutation H64Q with L29F results in a myoglobin with enhanced resistance to metMb formation in the absence of antioxidant enzymes (i.e. catalase and superoxide dismutase) due to its own high pseudoperoxidase activity, which rapidly removes any HOOH produced in the initial stages of autoxidation. Hydrogen Peroxide 257-261 myoglobin Physeter catodon 51-60 9407045-6 1997 Furthermore, Mb-I is found to be capable of performing two-electron oxidation of styrene, thioanisole, and H2O2. Hydrogen Peroxide 107-111 myoglobin Physeter catodon 13-17