PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15301945-5 2004 The immobilized Mb displayed good electrocatalytic responses to the reduction of both hydrogen peroxide (H(2)O(2)) and nitrite (NO(2)(-)), which were used to develop novel sensors for H(2)O(2) and NO(2)(-). Hydrogen Peroxide 86-103 myoglobin Homo sapiens 16-18 15526329-1 2004 Silver nanoparticles (11+/-1.5 nm) could greatly enhance the electron-transfer reactivity of myoglobin (Mb) and its catalytic ability toward hydrogen peroxide (H2O2). Hydrogen Peroxide 141-158 myoglobin Homo sapiens 93-102 15526329-1 2004 Silver nanoparticles (11+/-1.5 nm) could greatly enhance the electron-transfer reactivity of myoglobin (Mb) and its catalytic ability toward hydrogen peroxide (H2O2). Hydrogen Peroxide 141-158 myoglobin Homo sapiens 104-106 15526329-1 2004 Silver nanoparticles (11+/-1.5 nm) could greatly enhance the electron-transfer reactivity of myoglobin (Mb) and its catalytic ability toward hydrogen peroxide (H2O2). Hydrogen Peroxide 160-164 myoglobin Homo sapiens 93-102 15526329-1 2004 Silver nanoparticles (11+/-1.5 nm) could greatly enhance the electron-transfer reactivity of myoglobin (Mb) and its catalytic ability toward hydrogen peroxide (H2O2). Hydrogen Peroxide 160-164 myoglobin Homo sapiens 104-106 15136183-0 2004 An unmediated H2O2 biosensor based on the enzyme-like activity of myoglobin on multi-walled carbon nanotubes. Hydrogen Peroxide 14-18 myoglobin Homo sapiens 66-75 15035657-3 2004 Steady-state analyses of reaction mixtures containing Y103F Mb, purified linoleic acid and H2O2 revealed a lower total yield of lipid oxidation products than mixtures containing the wild-type protein, consistent with the reported decrease in the rate constant for reaction of Y103F Mb with H2O2 [Witting, Mauk and Lay (2002) Biochemistry 41, 11495-11503]. Hydrogen Peroxide 91-95 myoglobin Homo sapiens 282-284 12553846-2 2003 Ultrathin films (20-40 nm) containing myoglobin or cytochrome P450(cam) and DNA grown layer-by-layer on electrodes were activated by hydrogen peroxide, and the enzyme in the film generated metabolite styrene oxide from styrene. Hydrogen Peroxide 133-150 myoglobin Homo sapiens 38-47 15104207-10 2004 However, besides free iron-mediated free radical reactions, role of iron of higher oxidation states, formed during interaction of H2O2 with myoglobin might also be involved in oxidative degradation processes. Hydrogen Peroxide 130-134 myoglobin Homo sapiens 140-149 12952438-0 2003 Pseudoperoxidase activity of myoglobin: kinetics and mechanism of the peroxidase cycle of myoglobin with H2O2 and 2,2-azino-bis(3-ethylbenzthiazoline-6-sulfonate) as substrates. Hydrogen Peroxide 105-109 myoglobin Homo sapiens 29-38 12952438-0 2003 Pseudoperoxidase activity of myoglobin: kinetics and mechanism of the peroxidase cycle of myoglobin with H2O2 and 2,2-azino-bis(3-ethylbenzthiazoline-6-sulfonate) as substrates. Hydrogen Peroxide 105-109 myoglobin Homo sapiens 90-99 12952438-1 2003 Using 2,2-azino-bis(3-ethylbenzthiazoline-6-sulfonate) (ABTS) as substrate, it has been shown that the increased peroxidase activity for decreasing pH of myoglobin activated by hydrogen peroxide is due to a protonization of ferrylmyoglobin, MbFe(IV)=O, facilitating electron transfer from the substrate and corresponding to pK(a) approximately 5.2 at 25.0 degrees C and ionic strength 0.16, rather than due to specific acid catalysis. Hydrogen Peroxide 177-194 myoglobin Homo sapiens 154-163 12952438-5 2003 In contrast, the activation reaction between myoglobin and hydrogen peroxide was found at 25.0 degrees C to be slow and independent of pH with values of 171 +/- 7 and 196 +/- 19 M(-1) s(-1) found at physiological and meat pH, respectively, as determined by sequential stopped flow spectroscopy, from which a lower limit of k = 6 x 10(5) M(-1) s(-1) for the reaction between perferrylmyoglobin, .MbFe(IV)=O, and ABTS could be estimated. Hydrogen Peroxide 59-76 myoglobin Homo sapiens 45-54 12939145-1 2003 In the elucidation of structural requirements of heme vicinity for hydrogen peroxide activation, we found that the replacement of His-64 of myoglobin (Mb) with a negatively charged aspartate residue enhanced peroxidase and peroxygenase activities by 78- and 580-fold, respectively. Hydrogen Peroxide 67-84 myoglobin Homo sapiens 140-149 12702396-6 2002 Trichloroacetic acid, oxygen, and hydrogen peroxide were electrochemically catalyzed by [AQ/Mb](6) films with significant lowering of reduction overpotential. Hydrogen Peroxide 34-51 myoglobin Homo sapiens 92-94 12381195-8 2002 Cross-linked myoglobin-polyion films on pyrolytic graphite electrodes were used in strongly acidic solutions for the electrochemical catalytic reduction of trichloracetic acid, hydrogen peroxide, and oxygen. Hydrogen Peroxide 177-194 myoglobin Homo sapiens 13-22 10401602-2 1999 Myoglobin has not been viewed as a participant but is present in relatively high concentrations in heart muscle and, even under normal conditions, undergoes reactions that generate met (Fe3+) species and also superoxide, hydrogen peroxide, and other oxidants, albeit slowly. Hydrogen Peroxide 221-238 myoglobin Homo sapiens 0-9 11368929-0 2001 The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: a role for the protonated ferryl species. Hydrogen Peroxide 38-55 myoglobin Homo sapiens 95-104 10779502-0 2000 Reaction of human myoglobin and H2O2. Hydrogen Peroxide 32-36 myoglobin Homo sapiens 18-27 10720470-2 2000 Myoglobin in the presence of H(2)O(2) has been shown to catalyze LDL oxidation in vitro. Hydrogen Peroxide 29-37 myoglobin Homo sapiens 0-9 12236576-7 2002 Hematoporphyrin also increases the myoglobin-catalysed hydrogen peroxide-mediated oxidation of o-dianisidine and NADH. Hydrogen Peroxide 55-72 myoglobin Homo sapiens 35-44 11444837-5 2001 Both nitrite oxidation and tyrosine nitration were H(2)O(2)-dependent and required the formation of ferryl (Fe(+4)) myoglobin. Hydrogen Peroxide 51-59 myoglobin Homo sapiens 116-125 11226246-5 2001 Mb functions as a miniature chemical reactor, concentrating and orienting diatomic molecules such as NO, CO, O(2), and H(2)O(2) in highly conserved internal cavities. Hydrogen Peroxide 119-127 myoglobin Homo sapiens 0-2 10552907-2 1999 In the presence of an antioxidant, the ABTS(*+) radical-cation-forming chromogenic reaction, catalyzed by myoglobin and initiated by hydrogen peroxide (H(2)O(2)), has a lag period, and its duration is linearly correlated to the concentration of that antioxidant. Hydrogen Peroxide 133-150 myoglobin Homo sapiens 106-115 9839942-0 1998 The role of distal histidine in peroxidase activity of myoglobin--transient-kinetics study of the reaction of H2O2 with wild-type and distal-histidine-mutanted recombinant human myoglobin. Hydrogen Peroxide 110-114 myoglobin Homo sapiens 55-64 10563851-7 1999 In a membrane lipid peroxidation system, the effectiveness of the antioxidant was dependent on the catalyst: In the presence of H(2)O(2)-activated myoglobin, the inhibition efficiency of the antioxidant was malvidin 3-glucoside > catechin > malvidin > resveratrol. Hydrogen Peroxide 128-136 myoglobin Homo sapiens 147-156 9882417-1 1998 Treatment of myoglobin with H2O2 results in covalent alteration of the heme prosthetic group, in part, to protein-bound adducts. Hydrogen Peroxide 28-32 myoglobin Homo sapiens 13-22 9839942-0 1998 The role of distal histidine in peroxidase activity of myoglobin--transient-kinetics study of the reaction of H2O2 with wild-type and distal-histidine-mutanted recombinant human myoglobin. Hydrogen Peroxide 110-114 myoglobin Homo sapiens 178-187 9839942-3 1998 The effect of mutation of the distal histidine on the peroxidase activity of Mb has been investigated by stopped-flow kinetics of the reaction of hydrogen peroxide with wild-type Mb and [Gly64]Mb. Hydrogen Peroxide 146-163 myoglobin Homo sapiens 77-79 9839942-3 1998 The effect of mutation of the distal histidine on the peroxidase activity of Mb has been investigated by stopped-flow kinetics of the reaction of hydrogen peroxide with wild-type Mb and [Gly64]Mb. Hydrogen Peroxide 146-163 myoglobin Homo sapiens 179-181 9839942-3 1998 The effect of mutation of the distal histidine on the peroxidase activity of Mb has been investigated by stopped-flow kinetics of the reaction of hydrogen peroxide with wild-type Mb and [Gly64]Mb. Hydrogen Peroxide 146-163 myoglobin Homo sapiens 179-181 9839942-5 1998 The rate of reaction of H2O2 with the wild-type Mb decreased 8-9-fold on mutation of the distal histidine to glycine ([Gly64]Mb). Hydrogen Peroxide 24-28 myoglobin Homo sapiens 48-50 9839942-5 1998 The rate of reaction of H2O2 with the wild-type Mb decreased 8-9-fold on mutation of the distal histidine to glycine ([Gly64]Mb). Hydrogen Peroxide 24-28 myoglobin Homo sapiens 125-127 9839942-6 1998 A second slow phase was observed for the reaction of H2O2 with [Gly64]Mb, but was not observed in the corresponding reaction with wild-type Mb. Hydrogen Peroxide 53-57 myoglobin Homo sapiens 70-72 9839942-8 1998 The effect of pH on the rate of reaction of H2O2 with wild-type Mb and [Gly64]Mb is contrasting. Hydrogen Peroxide 44-48 myoglobin Homo sapiens 64-66 9839942-8 1998 The effect of pH on the rate of reaction of H2O2 with wild-type Mb and [Gly64]Mb is contrasting. Hydrogen Peroxide 44-48 myoglobin Homo sapiens 78-80 9839942-11 1998 The thermodynamic parameters calculated from the temperature-dependent study showed that the enthalpy of binding of H2O2 with Mb is positive, indicating that the process is endothermic. Hydrogen Peroxide 116-120 myoglobin Homo sapiens 126-128 9839942-12 1998 The apparent energy of activation of the reaction of H2O2 with Mb was found to be higher than that of peroxidases, suggesting that this may be oue of the reasons for the slower rate of the reaction of H2O2 with Mb compared with peroxidases. Hydrogen Peroxide 53-57 myoglobin Homo sapiens 63-65 9839942-12 1998 The apparent energy of activation of the reaction of H2O2 with Mb was found to be higher than that of peroxidases, suggesting that this may be oue of the reasons for the slower rate of the reaction of H2O2 with Mb compared with peroxidases. Hydrogen Peroxide 53-57 myoglobin Homo sapiens 211-213 9839942-12 1998 The apparent energy of activation of the reaction of H2O2 with Mb was found to be higher than that of peroxidases, suggesting that this may be oue of the reasons for the slower rate of the reaction of H2O2 with Mb compared with peroxidases. Hydrogen Peroxide 201-205 myoglobin Homo sapiens 63-65 9839942-12 1998 The apparent energy of activation of the reaction of H2O2 with Mb was found to be higher than that of peroxidases, suggesting that this may be oue of the reasons for the slower rate of the reaction of H2O2 with Mb compared with peroxidases. Hydrogen Peroxide 201-205 myoglobin Homo sapiens 211-213 9667493-1 1998 The oxidation of adrenaline by ferrylmyoglobin, the product formed by the oxidation of myoglobin with H2O2, was examined by absorption, fluorescence, and EPR spectroscopy in terms of the formation of intermediate free radicals and stable molecular products and the binding of adrenaline oxidation products to the apoprotein. Hydrogen Peroxide 102-106 myoglobin Homo sapiens 37-46 9706741-12 1998 We conclude that in the presence of a hemoprotein such as myoglobin or hemoglobin, NO may promote or inhibit oxidation reactions depending upon the relative fluxes of O2-, H2O2, and NO. Hydrogen Peroxide 172-176 myoglobin Homo sapiens 58-67 9494102-1 1998 The reaction between myoglobin and the lipid hydroperoxide 13(S)-hydroperoxy-9,11(cis,trans)-octadecadienoic acid (HPODE) was studied kinetically by spectrophotometric, polarographic and analytical methods. Hydrogen Peroxide 45-58 myoglobin Homo sapiens 21-30 9367178-4 1997 ESR measurements at 77 K showed the formation of the ferrous nitrosyl myoglobin, Mb-NO, in the reaction mixtures containing Mb, H2O2 and HA. Hydrogen Peroxide 128-132 myoglobin Homo sapiens 70-79 9367178-4 1997 ESR measurements at 77 K showed the formation of the ferrous nitrosyl myoglobin, Mb-NO, in the reaction mixtures containing Mb, H2O2 and HA. Hydrogen Peroxide 128-132 myoglobin Homo sapiens 81-83 9367178-5 1997 Our data also demonstrate that Mb-NO is an end product of the reaction pathway involving Mb, H2O2 and HA, rather than a reaction intermediate in the formation of NO. Hydrogen Peroxide 93-97 myoglobin Homo sapiens 31-33 9025973-4 1997 Under optimal conditions of 0.53 mM O-dianisidine, 0.15 mM H2O2, pH 6.0, either myoglobin or hemoglobin produced absorbance at 460 nm in a concentration-dependent manner similar to that of MPO. Hydrogen Peroxide 59-63 myoglobin Homo sapiens 80-89 8521861-1 1995 Met-myoglobin [Fe(III)] was found to induce myosin cross-linking in the presence of H2O2 [Bhoite-Solomon, V. & Shaklai, N. (1992) Biochem. Hydrogen Peroxide 84-88 myoglobin Homo sapiens 4-13 8791091-0 1996 Covalent crosslinking of the heme prosthetic group to myoglobin by H2O2: toxicological implications. Hydrogen Peroxide 67-71 myoglobin Homo sapiens 54-63 8791091-1 1996 It is known that treatment of myoglobin with H2O2 leads to covalent alteration of the heme prosthetic group with concomitant formation of a protein bound heme adduct and transforms myoglobin from an oxygen storage protein to an oxidase. Hydrogen Peroxide 45-49 myoglobin Homo sapiens 30-39 8791091-1 1996 It is known that treatment of myoglobin with H2O2 leads to covalent alteration of the heme prosthetic group with concomitant formation of a protein bound heme adduct and transforms myoglobin from an oxygen storage protein to an oxidase. Hydrogen Peroxide 45-49 myoglobin Homo sapiens 181-190 8521861-9 1995 Addition of myoglobin/H2O2 to high myosin concentrations (> = 20 microM) turned the solutions into gels, a phenomenon explained by the further formation of intermolecular super cross-links of soluble myosin. Hydrogen Peroxide 22-26 myoglobin Homo sapiens 12-21 7889144-1 1995 The 5,5-dimethyl-1-pyrroline-N-oxide (DMPO) spin adduct of myoglobin (Mb) or hemoglobin (Hb) was formed when metmyoglobin (MetMb) or methemoglobin (MetHb) reacted with H2O2 in the presence of DMPO, and both decayed with half-life of a few minutes. Hydrogen Peroxide 168-172 myoglobin Homo sapiens 59-68 7889144-1 1995 The 5,5-dimethyl-1-pyrroline-N-oxide (DMPO) spin adduct of myoglobin (Mb) or hemoglobin (Hb) was formed when metmyoglobin (MetMb) or methemoglobin (MetHb) reacted with H2O2 in the presence of DMPO, and both decayed with half-life of a few minutes. Hydrogen Peroxide 168-172 myoglobin Homo sapiens 70-72 7889144-8 1995 The decay rate of the spin adduct of Mb was increased by hematin in the presence of H2O2 and decreased by catalase. Hydrogen Peroxide 84-88 myoglobin Homo sapiens 37-39 7889144-10 1995 These results led us to conclude that instability of the DMPO-spin adducts of Mb and Hb is due to intramolecular redox reactions between the spin adducts and amino acid residues and/or products of the reaction between heme and H2O2. Hydrogen Peroxide 227-231 myoglobin Homo sapiens 78-80 8386688-4 1993 From the evidence of these and other experiments it was concluded that the DMPO-OH adduct reacts with hydrogen peroxide and myoglobin to give non-paramagnetic products, and hence that the use of the DMPO spin trap to detect hydroxyl or other active radicals in systems containing physiological concentrations of myoglobin may give misleading results. Hydrogen Peroxide 102-119 myoglobin Homo sapiens 312-321 8125965-0 1994 Reaction of myoglobin with hydrogen peroxide forms a peroxyl radical which oxidizes substrates. Hydrogen Peroxide 27-44 myoglobin Homo sapiens 12-21 8125965-1 1994 Evidence is presented that the radical observed upon reaction of myoglobin with hydrogen peroxide is a peroxyl radical. Hydrogen Peroxide 80-97 myoglobin Homo sapiens 65-74 8454048-0 1993 Myoglobin protects against endothelial cell membrane damage associated with hydrogen peroxide or xanthine/xanthine oxidase. Hydrogen Peroxide 76-93 myoglobin Homo sapiens 0-9 8241712-0 1993 Antioxidant effect of coenzyme Q on hydrogen peroxide-activated myoglobin. Hydrogen Peroxide 36-53 myoglobin Homo sapiens 64-73 7811298-1 1994 A mixture of myoglobin and hydrogen peroxide (H2O2) causes peroxidation of arachidonic acid. Hydrogen Peroxide 46-50 myoglobin Homo sapiens 13-22 1309791-8 1992 The contribution of either direct electron transfer to the heme iron or nucleophilic addition depended on the physicochemical properties of the thiol involved and on the availability of H2O2 to reoxidize met-myoglobin to ferrylmyoglobin. Hydrogen Peroxide 186-190 myoglobin Homo sapiens 208-217 1420896-0 1992 Hydrogen peroxide plays a key role in the oxidation reaction of myoglobin by molecular oxygen. Hydrogen Peroxide 0-17 myoglobin Homo sapiens 64-73 33821889-6 2021 Ag/AgCl reference electrode, in the presence of hydrogen peroxide, indicated an additional H-bonding in the mutant protein, which is responsible for the peroxidase activity of the mutant Mb. Hydrogen Peroxide 48-65 myoglobin Homo sapiens 187-189 2368504-2 1990 A method for the sensitive determination of myoglobin in the extracts was developed based on its ability to form a red dye by the oxidative coupling of 2,4-dichlorophenol and 4-aminoantipyrine in the presence of hydrogen peroxide. Hydrogen Peroxide 212-229 myoglobin Homo sapiens 44-53 1654842-4 1991 Myoglobin in several forms such as metmyoglobin, oxymyoglobin, and nitric oxide-myoglobin were interacted with an equimolar concentration of hydrogen peroxide. Hydrogen Peroxide 141-158 myoglobin Homo sapiens 0-9 1654842-4 1991 Myoglobin in several forms such as metmyoglobin, oxymyoglobin, and nitric oxide-myoglobin were interacted with an equimolar concentration of hydrogen peroxide. Hydrogen Peroxide 141-158 myoglobin Homo sapiens 38-47 1654842-6 1991 The results showed that metmyoglobin and oxymyoglobin were activated by H2O2 to ferryl myoglobin, which initiates membrane lipid peroxidation; but not nitric oxide-myoglobin, which, during interaction with H2O2, did not form ferryl but metmyoglobin which only poorly affected lipid peroxidation. Hydrogen Peroxide 72-76 myoglobin Homo sapiens 27-36 1654842-6 1991 The results showed that metmyoglobin and oxymyoglobin were activated by H2O2 to ferryl myoglobin, which initiates membrane lipid peroxidation; but not nitric oxide-myoglobin, which, during interaction with H2O2, did not form ferryl but metmyoglobin which only poorly affected lipid peroxidation. Hydrogen Peroxide 72-76 myoglobin Homo sapiens 44-53 1654842-6 1991 The results showed that metmyoglobin and oxymyoglobin were activated by H2O2 to ferryl myoglobin, which initiates membrane lipid peroxidation; but not nitric oxide-myoglobin, which, during interaction with H2O2, did not form ferryl but metmyoglobin which only poorly affected lipid peroxidation. Hydrogen Peroxide 206-210 myoglobin Homo sapiens 27-36 1654842-6 1991 The results showed that metmyoglobin and oxymyoglobin were activated by H2O2 to ferryl myoglobin, which initiates membrane lipid peroxidation; but not nitric oxide-myoglobin, which, during interaction with H2O2, did not form ferryl but metmyoglobin which only poorly affected lipid peroxidation. Hydrogen Peroxide 206-210 myoglobin Homo sapiens 44-53 1651705-1 1991 The interaction of myoglobin with H2O2 leads via a two-electron oxidation process to the formation of ferryl myoglobin. Hydrogen Peroxide 34-38 myoglobin Homo sapiens 19-28 1651705-1 1991 The interaction of myoglobin with H2O2 leads via a two-electron oxidation process to the formation of ferryl myoglobin. Hydrogen Peroxide 34-38 myoglobin Homo sapiens 109-118 33821889-7 2021 We observed that in the presence of 5 mM H2O2, H64DOPA Mb oxidizes thioanisole and benzaldehyde with a 10 and 54 folds higher rate, respectively, as opposed to WT Mb. Hydrogen Peroxide 41-45 myoglobin Homo sapiens 55-57 33821889-7 2021 We observed that in the presence of 5 mM H2O2, H64DOPA Mb oxidizes thioanisole and benzaldehyde with a 10 and 54 folds higher rate, respectively, as opposed to WT Mb. Hydrogen Peroxide 41-45 myoglobin Homo sapiens 163-165 35563217-0 2022 Reactivity of Myoglobin Reconstituted with Cobalt Corrole toward Hydrogen Peroxide. Hydrogen Peroxide 65-82 myoglobin Homo sapiens 14-23 34671319-9 2021 MB knockdown also led to higher reactive oxygen species (ROS) levels in the cells after treatment with H2O2. Hydrogen Peroxide 103-107 myoglobin Homo sapiens 0-2 34243819-6 2021 In a model reaction of Mb + EtOH + H2O2, we observed time-dependent AcAld formation. Hydrogen Peroxide 35-39 myoglobin Homo sapiens 23-25 2775230-1 1989 The reaction product of myoglobin and H2O2 exists in two different forms according to the external pH. Hydrogen Peroxide 38-42 myoglobin Homo sapiens 24-33 32599765-1 2020 Myoglobin (Mb), an oxygen-binding heme protein highly expressed in heart and skeletal muscle, has been shown to undergo oxidative modifications on both an inter- and intramolecular level when exposed to hydrogen peroxide (H2O2) in vitro. Hydrogen Peroxide 203-220 myoglobin Homo sapiens 0-9 2744579-1 1989 Met-myoglobin is oxidized both by H2O2 and other hydroperoxides to a species with a higher iron valency state and the spectral characteristics of ferryl-myoglobin. Hydrogen Peroxide 34-38 myoglobin Homo sapiens 4-13 2744579-1 1989 Met-myoglobin is oxidized both by H2O2 and other hydroperoxides to a species with a higher iron valency state and the spectral characteristics of ferryl-myoglobin. Hydrogen Peroxide 49-63 myoglobin Homo sapiens 4-13 3199797-0 1988 Modulation of myoglobin-H2O2-mediated peroxidation reactions by sulfhydryl compounds. Hydrogen Peroxide 24-28 myoglobin Homo sapiens 14-23 3199797-1 1988 The ability of specific low molecular weight sulfhydryl compounds to inhibit the myoglobin-H2O2 peroxidation of uric acid and arachidonic acid was investigated. Hydrogen Peroxide 91-95 myoglobin Homo sapiens 81-90 3199797-5 1988 Under conditions of this assay, the ferrous form of myoglobin and H2O2 produced approximately three times the amount of formaldehyde from dimethylsulfoxide than ferric myoglobin (metmyoglobin) and H2O2. Hydrogen Peroxide 66-70 myoglobin Homo sapiens 168-177 3199797-5 1988 Under conditions of this assay, the ferrous form of myoglobin and H2O2 produced approximately three times the amount of formaldehyde from dimethylsulfoxide than ferric myoglobin (metmyoglobin) and H2O2. Hydrogen Peroxide 197-201 myoglobin Homo sapiens 52-61 3199797-8 1988 Visible absorption spectra of oxymyoglobin and metmyoglobin after incubation with H2O2 indicates the formation of a relatively stable ferriperoxide derivative of myoglobin. Hydrogen Peroxide 82-86 myoglobin Homo sapiens 33-42 3199797-10 1988 These data are consistent with the hypothesis that during reperfusion injury of the ischemic myocardium, the phagocytic cell or intracellular-derived H2O2 may react with myoglobin and initiate peroxidation reactions independent of .OH formation leading to cell injury. Hydrogen Peroxide 150-154 myoglobin Homo sapiens 170-179 3199797-11 1988 The cardioprotective effects of alpha-mercaptopropionyl glycine and other sulfhydryl-containing compounds during reperfusion injury may be attributed, at least in part, to their ability to inhibit myoglobin-H2O2-mediated peroxidation reactions. Hydrogen Peroxide 207-211 myoglobin Homo sapiens 197-206 3939140-0 1985 Myoglobin-catalyzed hydrogen peroxide dependent arachidonic acid peroxidation. Hydrogen Peroxide 20-37 myoglobin Homo sapiens 0-9 3939140-3 1985 To understand fully the interaction between reactive oxygen metabolites, myoglobin and lipid, we investigate the possibility that myoglobin may use xanthine oxidase-generated superoxide and/or hydrogen peroxide to catalyze peroxidation of a polyunsaturated fatty acid. Hydrogen Peroxide 193-210 myoglobin Homo sapiens 130-139 32957872-2 2021 This study was undertaken to investigation the role of hydrogen peroxide (H2O2) in the formation of met-myoglobin and the protective potential of four different reductants such as uric acid, folic acid, glutathione and ascorbic acid were also tested against met-myoglobin formation. Hydrogen Peroxide 55-72 myoglobin Homo sapiens 104-113 32957872-2 2021 This study was undertaken to investigation the role of hydrogen peroxide (H2O2) in the formation of met-myoglobin and the protective potential of four different reductants such as uric acid, folic acid, glutathione and ascorbic acid were also tested against met-myoglobin formation. Hydrogen Peroxide 55-72 myoglobin Homo sapiens 262-271 32957872-2 2021 This study was undertaken to investigation the role of hydrogen peroxide (H2O2) in the formation of met-myoglobin and the protective potential of four different reductants such as uric acid, folic acid, glutathione and ascorbic acid were also tested against met-myoglobin formation. Hydrogen Peroxide 74-78 myoglobin Homo sapiens 104-113 32957872-3 2021 METHODS: Human myoglobin was treated with H2O2 in-vitro in order to prepare met-myoglobin. Hydrogen Peroxide 42-46 myoglobin Homo sapiens 15-24 32957872-3 2021 METHODS: Human myoglobin was treated with H2O2 in-vitro in order to prepare met-myoglobin. Hydrogen Peroxide 42-46 myoglobin Homo sapiens 80-89 32957872-4 2021 The generation of metmyoglobin was confirmed by UV-visible spectroscopy and its stability was analysed by the treatment of human myoglobin with H2O2 at varying pH or time. Hydrogen Peroxide 144-148 myoglobin Homo sapiens 21-30 32957872-7 2021 RESULTS: The novel data of this study showed that H2O2 induced extensive damage of myoglobin but the treatment with uric acid, folic acid, glutathione or ascorbic acid provides protection of myoglobin against H2O2 induced oxidative damaged. Hydrogen Peroxide 50-54 myoglobin Homo sapiens 83-92 32957872-7 2021 RESULTS: The novel data of this study showed that H2O2 induced extensive damage of myoglobin but the treatment with uric acid, folic acid, glutathione or ascorbic acid provides protection of myoglobin against H2O2 induced oxidative damaged. Hydrogen Peroxide 209-213 myoglobin Homo sapiens 191-200 2806954-4 1989 The results show that iron release from ferrimyoglobin activated by hydrogen peroxide is suppressed in the presence of membranes, apparently by the reduction of the ferryl myoglobin species, and lipid peroxidation occurs. Hydrogen Peroxide 68-85 myoglobin Homo sapiens 45-54 3939140-6 1985 Inhibition studies reveal that myoglobin uses hydrogen peroxide, not superoxide to form either an oxo-heme-oxidant or caged radical that initiates arachidonate peroxidation. Hydrogen Peroxide 46-63 myoglobin Homo sapiens 31-40 32599765-1 2020 Myoglobin (Mb), an oxygen-binding heme protein highly expressed in heart and skeletal muscle, has been shown to undergo oxidative modifications on both an inter- and intramolecular level when exposed to hydrogen peroxide (H2O2) in vitro. Hydrogen Peroxide 222-226 myoglobin Homo sapiens 0-9 29594482-0 2018 Myoglobin immobilized on mesoporous carbon foam in a hydrogel (selep) dispersant for voltammetric sensing of hydrogen peroxide. Hydrogen Peroxide 109-126 myoglobin Homo sapiens 0-9 32436700-3 2020 In this study, we examined the ability of myoglobin to produce HNO via the peroxidation of hydroxylamine with H2O2 using both experimental and computational approaches. Hydrogen Peroxide 110-114 myoglobin Homo sapiens 42-51 31901702-0 2020 Low frequency magnetic fields modification on hydrogen peroxide oxidized myoglobin-isolate and mechanisms underlying the chain reaction process. Hydrogen Peroxide 46-63 myoglobin Homo sapiens 73-82 26656812-6 2015 Hydrogen peroxide, oxygen, and nitrite were electrochemically catalyzed by the Mb-CA"s composite film with significant lowering of the reduction overpotential. Hydrogen Peroxide 0-17 myoglobin Homo sapiens 79-81 27019153-6 2016 Experimental data demonstrated that the electron transfer between Mb and electrode was greatly facilitated and showed good electrocatalytic properties toward various substrates, such as H2O2 and NaNO2, with significant lowering of reduction overpotential. Hydrogen Peroxide 186-190 myoglobin Homo sapiens 66-68 25262340-0 2015 MWCNT-cysteamine-Nafion modified gold electrode based on myoglobin for determination of hydrogen peroxide and nitrite. Hydrogen Peroxide 88-105 myoglobin Homo sapiens 57-66 25262340-1 2015 In this work, a novel amperometric biosensor of hydrogen peroxide (H2O2) was developed based on the immobilization of myoglobin (Mb) on the surface of the multi-walled carbon nanotube (MWCNT) -Nafion-cysteamine (CA) modified gold electrode (Au) and its electrocatalytic activity was used for the determination of nitrite (NO2(-)). Hydrogen Peroxide 48-65 myoglobin Homo sapiens 118-127 25262340-1 2015 In this work, a novel amperometric biosensor of hydrogen peroxide (H2O2) was developed based on the immobilization of myoglobin (Mb) on the surface of the multi-walled carbon nanotube (MWCNT) -Nafion-cysteamine (CA) modified gold electrode (Au) and its electrocatalytic activity was used for the determination of nitrite (NO2(-)). Hydrogen Peroxide 67-71 myoglobin Homo sapiens 118-127 27955988-0 2017 Electrochemical H2O2 biosensor composed of myoglobin on MoS2 nanoparticle-graphene oxide hybrid structure. Hydrogen Peroxide 16-20 myoglobin Homo sapiens 43-52 27955988-1 2017 In this research, the electrochemical biosensor composed of myoglobin (Mb) on molybdenum disulfide nanoparticles (MoS2 NP) encapsulated with graphene oxide (GO) was fabricated for the detection of hydrogen peroxide (H2O2). Hydrogen Peroxide 197-214 myoglobin Homo sapiens 60-69 27955988-1 2017 In this research, the electrochemical biosensor composed of myoglobin (Mb) on molybdenum disulfide nanoparticles (MoS2 NP) encapsulated with graphene oxide (GO) was fabricated for the detection of hydrogen peroxide (H2O2). Hydrogen Peroxide 197-214 myoglobin Homo sapiens 71-73 27955988-1 2017 In this research, the electrochemical biosensor composed of myoglobin (Mb) on molybdenum disulfide nanoparticles (MoS2 NP) encapsulated with graphene oxide (GO) was fabricated for the detection of hydrogen peroxide (H2O2). Hydrogen Peroxide 216-220 myoglobin Homo sapiens 60-69 27955988-1 2017 In this research, the electrochemical biosensor composed of myoglobin (Mb) on molybdenum disulfide nanoparticles (MoS2 NP) encapsulated with graphene oxide (GO) was fabricated for the detection of hydrogen peroxide (H2O2). Hydrogen Peroxide 216-220 myoglobin Homo sapiens 71-73 27955988-3 2017 As a sensing material, Mb was introduced to fabricate the biosensor for H2O2 detection. Hydrogen Peroxide 72-76 myoglobin Homo sapiens 23-25 24211453-0 2014 Direct electrochemistry of myoglobin at reduced graphene oxide-multiwalled carbon nanotubes-platinum nanoparticles nanocomposite and biosensing towards hydrogen peroxide and nitrite. Hydrogen Peroxide 152-169 myoglobin Homo sapiens 27-36 24211453-1 2014 We described the preparation of a novel nanobiocomposite, reduced graphene oxide- multiwalled carbon nanotubes-platinum nanoparticles/myoglobin (RGO-MWCNT-Pt/Mb) for the direct electrochemistry of myoglobin and its application towards determination of hydrogen peroxide (H2O2) and nitrite (NO2(-)). Hydrogen Peroxide 252-269 myoglobin Homo sapiens 134-143 23488820-1 2013 Magnetic hybrid assemblies of Ag and Fe3O4 nanoparticles with biocompatibly immobilized myoglobin (Mb) were designed to detect and capture toxic targets (NO2-, CN-, and H2O2). Hydrogen Peroxide 169-173 myoglobin Homo sapiens 88-97 24211453-1 2014 We described the preparation of a novel nanobiocomposite, reduced graphene oxide- multiwalled carbon nanotubes-platinum nanoparticles/myoglobin (RGO-MWCNT-Pt/Mb) for the direct electrochemistry of myoglobin and its application towards determination of hydrogen peroxide (H2O2) and nitrite (NO2(-)). Hydrogen Peroxide 252-269 myoglobin Homo sapiens 197-206 24211453-1 2014 We described the preparation of a novel nanobiocomposite, reduced graphene oxide- multiwalled carbon nanotubes-platinum nanoparticles/myoglobin (RGO-MWCNT-Pt/Mb) for the direct electrochemistry of myoglobin and its application towards determination of hydrogen peroxide (H2O2) and nitrite (NO2(-)). Hydrogen Peroxide 271-275 myoglobin Homo sapiens 134-143 24211453-1 2014 We described the preparation of a novel nanobiocomposite, reduced graphene oxide- multiwalled carbon nanotubes-platinum nanoparticles/myoglobin (RGO-MWCNT-Pt/Mb) for the direct electrochemistry of myoglobin and its application towards determination of hydrogen peroxide (H2O2) and nitrite (NO2(-)). Hydrogen Peroxide 271-275 myoglobin Homo sapiens 197-206 23608540-1 2013 In this study, an enzymatic biosensor for amperometric detection of hydrogen peroxide was developed based on the direct electrochemistry of myoglobin (Mb) on a porous cerium dioxide (CeO2) nanostructured film. Hydrogen Peroxide 68-85 myoglobin Homo sapiens 140-149 23608540-1 2013 In this study, an enzymatic biosensor for amperometric detection of hydrogen peroxide was developed based on the direct electrochemistry of myoglobin (Mb) on a porous cerium dioxide (CeO2) nanostructured film. Hydrogen Peroxide 68-85 myoglobin Homo sapiens 151-153 24205675-0 2013 An electrochemical H2O2 detection method based on direct electrochemistry of myoglobin immobilized on gold deposited ITO electrode. Hydrogen Peroxide 19-23 myoglobin Homo sapiens 77-86 24205675-1 2013 A protein based electrochemical sensor for the detection of hydrogen peroxide based on Myoglobin immobilized on gold nano structures patterned on Indium tin oxide electrode was developed. Hydrogen Peroxide 60-77 myoglobin Homo sapiens 87-96 23575474-0 2013 Effect of distal histidines on hydrogen peroxide activation by manganese reconstituted myoglobin. Hydrogen Peroxide 31-48 myoglobin Homo sapiens 87-96 23575474-2 2013 In this work, we reconstituted myoglobin by the replacement of natural heme with manganese(iii) protoporphyrin IX and firstly investigated the effect of distal histidine on the reaction of Mn(III) porphyrin with H2O2 and one-electron oxidation of ABTS. Hydrogen Peroxide 212-216 myoglobin Homo sapiens 31-40 23488820-1 2013 Magnetic hybrid assemblies of Ag and Fe3O4 nanoparticles with biocompatibly immobilized myoglobin (Mb) were designed to detect and capture toxic targets (NO2-, CN-, and H2O2). Hydrogen Peroxide 169-173 myoglobin Homo sapiens 99-101 23109864-5 2012 With o-dianisidine and H(2)O(2) as the substrate, the peroxidase activity of adsorbed myoglobin was determined. Hydrogen Peroxide 23-31 myoglobin Homo sapiens 86-95 23576844-7 2012 Mb in the films displayed good electrocatalytic activities towards various substrates such as hydrogen peroxide, nitrite and oxygen, indicating that the composite films have potential applications in fabricating novel biosensors without using mediators. Hydrogen Peroxide 94-111 myoglobin Homo sapiens 0-2 21609760-0 2011 Myoglobin-H2O2 catalyzes the oxidation of beta-ketoacids to alpha-dicarbonyls: mechanism and implications in ketosis. Hydrogen Peroxide 10-14 myoglobin Homo sapiens 0-9 22097860-0 2011 [Comparison between myoglobin and its mutant(D60K) interacting with hydrogen peroxide by spectrum]. Hydrogen Peroxide 68-85 myoglobin Homo sapiens 20-29 21609760-11 2011 The generation of radicals and triplet dicarbonyl products by Mb/H(2)O(2)/beta-ketoacids may contribute to the adverse health effects of ketogenic unbalance. Hydrogen Peroxide 65-73 myoglobin Homo sapiens 62-64 19735144-6 2009 The enzymatic activity of the nanostructured biocomposite was evaluated in the oxidation of 2-methoxyphenol by hydrogen peroxide and discussed on the basis of structural properties of adsorbed myoglobin. Hydrogen Peroxide 111-128 myoglobin Homo sapiens 193-202 20230770-0 2010 Hydrogen peroxide biosensor based on a myoglobin/hydrophilic room temperature ionic liquid film. Hydrogen Peroxide 0-17 myoglobin Homo sapiens 39-48 19942425-4 2010 The modified electrode based on this Mb/Fe(3)O(4)@Au biofilm displayed good electrocatalytic activity to the reduction of H(2)O(2) with a linear range from 1.28 to 283 microM. Hydrogen Peroxide 122-130 myoglobin Homo sapiens 37-39 19188096-4 2009 Mb in the {PEG/ZrO(2)}(n)-Mb films fabricated on pyrolytic graphite (PG) electrodes showed direct and quasi-reversible CV response, which could be used to electrocatalyze reduction of oxygen and hydrogen peroxide. Hydrogen Peroxide 195-212 myoglobin Homo sapiens 0-2 19557774-0 2009 Noncovalent modulation of pH-dependent reactivity of a Mn-salen cofactor in myoglobin with hydrogen peroxide. Hydrogen Peroxide 91-108 myoglobin Homo sapiens 76-85 19394899-5 2009 The Nafion/Mb/MWCNTs/CILE gave excellent electrocatalytic activity towards different substrates including trichloroacetic acid (TCA), hydrogen peroxide (H(2)O(2)) and sodium nitrite (NaNO(2)). Hydrogen Peroxide 134-151 myoglobin Homo sapiens 11-13 19185484-0 2009 Cathodic detection of H2O2 based on nanopyramidal gold surface with enhanced electron transfer of myoglobin. Hydrogen Peroxide 22-26 myoglobin Homo sapiens 98-107 19185484-2 2009 Electrochemical investigation indicates that Mb is stably confined on the nanopyramidal gold surface and maintains electrocatalytic activity toward hydrogen peroxide (H(2)O(2)). Hydrogen Peroxide 148-165 myoglobin Homo sapiens 45-47 19188096-4 2009 Mb in the {PEG/ZrO(2)}(n)-Mb films fabricated on pyrolytic graphite (PG) electrodes showed direct and quasi-reversible CV response, which could be used to electrocatalyze reduction of oxygen and hydrogen peroxide. Hydrogen Peroxide 195-212 myoglobin Homo sapiens 26-28 19437988-3 2009 The Mb-loaded films at pyrolytic graphite (PG) electrodes, designated as {PA/ZrO2}n-Mb, demonstrated well-defined and quasi-reversible CV responses for Mb Fe(III)/Fe(II) redox couple and good electrocatalytic properties toward oxygen and H2O2. Hydrogen Peroxide 238-242 myoglobin Homo sapiens 4-6 19109005-0 2009 Hydrogen peroxide biosensor based on the direct electrochemistry of myoglobin immobilized on silver nanoparticles doped carbon nanotubes film. Hydrogen Peroxide 0-17 myoglobin Homo sapiens 68-77 19109005-1 2009 A novel H(2)O(2) biosensor has been fabricated based on the direct electrochemistry and electrocatalysis of myoglobin (Mb) immobilized on silver nanoparticles doped carbon nanotubes film with hybrid sol-gel techniques. Hydrogen Peroxide 8-16 myoglobin Homo sapiens 108-117 19109005-1 2009 A novel H(2)O(2) biosensor has been fabricated based on the direct electrochemistry and electrocatalysis of myoglobin (Mb) immobilized on silver nanoparticles doped carbon nanotubes film with hybrid sol-gel techniques. Hydrogen Peroxide 8-16 myoglobin Homo sapiens 119-121 17561388-4 2007 {PPI-Au/Mb}(n) films on PG electrodes demonstrated a pair of well-defined and quasi-reversible CV reduction-oxidation peaks for Mb heme Fe(III)/Fe(II) couple and good electrocatalytic properties toward reduction of oxygen and hydrogen peroxide. Hydrogen Peroxide 226-243 myoglobin Homo sapiens 8-10 18829300-7 2009 The biocatalytic activity of Mb in the composite film was exemplified by the reduction of hydrogen peroxide. Hydrogen Peroxide 90-107 myoglobin Homo sapiens 29-31 18321683-0 2008 Direct electron-transfer of myoglobin within a new zwitterionic gemini surfactant film and its analytical application for H2O2 detection. Hydrogen Peroxide 122-126 myoglobin Homo sapiens 28-37 18321683-4 2008 The presence of hydrogen peroxide changed the typical electrochemical behaviors in terms of bioelectrocatalysis of myoglobin to hydrogen peroxide, and a higher sensitive electroanalytical method for the determination of hydrogen peroxide has been developed. Hydrogen Peroxide 16-33 myoglobin Homo sapiens 115-124 18321683-4 2008 The presence of hydrogen peroxide changed the typical electrochemical behaviors in terms of bioelectrocatalysis of myoglobin to hydrogen peroxide, and a higher sensitive electroanalytical method for the determination of hydrogen peroxide has been developed. Hydrogen Peroxide 128-145 myoglobin Homo sapiens 115-124 18321683-4 2008 The presence of hydrogen peroxide changed the typical electrochemical behaviors in terms of bioelectrocatalysis of myoglobin to hydrogen peroxide, and a higher sensitive electroanalytical method for the determination of hydrogen peroxide has been developed. Hydrogen Peroxide 128-145 myoglobin Homo sapiens 115-124 17875390-4 2007 Compared with the Mb-MCFs/GC electrode, the Mb-QDs-MCFs/GC electrode could not only realize enhanced direct electrochemistry but also display better sensitivity and wider linear range to the detection of hydrogen peroxide. Hydrogen Peroxide 204-221 myoglobin Homo sapiens 18-20 17875390-4 2007 Compared with the Mb-MCFs/GC electrode, the Mb-QDs-MCFs/GC electrode could not only realize enhanced direct electrochemistry but also display better sensitivity and wider linear range to the detection of hydrogen peroxide. Hydrogen Peroxide 204-221 myoglobin Homo sapiens 44-46 17939657-3 2007 Treating oxyHb with peroxynitrite and Mb with H2O2 in the presence of a low DMPO concentration yielded secondary Cys-DMPO radical adduct exclusively, whereas in the presence of high DMPO, more of the primary Tyr-DMPO radical adduct was detected. Hydrogen Peroxide 46-50 myoglobin Homo sapiens 38-40 17561388-4 2007 {PPI-Au/Mb}(n) films on PG electrodes demonstrated a pair of well-defined and quasi-reversible CV reduction-oxidation peaks for Mb heme Fe(III)/Fe(II) couple and good electrocatalytic properties toward reduction of oxygen and hydrogen peroxide. Hydrogen Peroxide 226-243 myoglobin Homo sapiens 128-130 16887098-0 2006 Expression of human myoglobin in H9c2 cells enhances toxicity to added hydrogen peroxide. Hydrogen Peroxide 71-88 myoglobin Homo sapiens 20-29 17637042-2 2007 Specifically, the nature of the radicals on human myoglobin induced by the addition of hydrogen peroxide and captured by the spin trap 5,5-dimethyl-1-pyrroline N-oxide (DMPO) was investigated. Hydrogen Peroxide 87-104 myoglobin Homo sapiens 50-59 16887098-2 2006 Myoglobin (Mb) is present in CM at significant concentrations and reacts with H2O2 to yield one- and two-electron oxidants that may promote myocardial injury. Hydrogen Peroxide 78-82 myoglobin Homo sapiens 0-9 16887098-2 2006 Myoglobin (Mb) is present in CM at significant concentrations and reacts with H2O2 to yield one- and two-electron oxidants that may promote myocardial injury. Hydrogen Peroxide 78-82 myoglobin Homo sapiens 11-13 16887098-7 2006 Contrary to expectation, cells expressing WT or the Y103F Mb show increased mitochondrial dysfunction and apoptosis, and decreased ATP in response to H2O2 that follows the order native < Y103F Mb < WT human Mb consistent with the increasing pro-oxidant activity for these proteins. Hydrogen Peroxide 150-154 myoglobin Homo sapiens 58-60 16887098-7 2006 Contrary to expectation, cells expressing WT or the Y103F Mb show increased mitochondrial dysfunction and apoptosis, and decreased ATP in response to H2O2 that follows the order native < Y103F Mb < WT human Mb consistent with the increasing pro-oxidant activity for these proteins. Hydrogen Peroxide 150-154 myoglobin Homo sapiens 196-198 16887098-7 2006 Contrary to expectation, cells expressing WT or the Y103F Mb show increased mitochondrial dysfunction and apoptosis, and decreased ATP in response to H2O2 that follows the order native < Y103F Mb < WT human Mb consistent with the increasing pro-oxidant activity for these proteins. Hydrogen Peroxide 150-154 myoglobin Homo sapiens 196-198 16430850-3 2006 Moreover, the entrapped Mb realized direct electron transfer with the electrode and displayed an elegant catalytic activity toward the reduction of hydrogen peroxide, nitrite, and trichloroacetic acid, by which the mediator-free biosensors could be fabricated. Hydrogen Peroxide 148-165 myoglobin Homo sapiens 24-26 16216040-0 2006 Easy oxidation and nitration of human myoglobin by nitrite and hydrogen peroxide. Hydrogen Peroxide 63-80 myoglobin Homo sapiens 38-47 16216040-1 2006 The modification of human myoglobin (HMb) by reaction with nitrite and hydrogen peroxide has been investigated. Hydrogen Peroxide 71-88 myoglobin Homo sapiens 26-35 16471801-4 2006 Compared with other Mb layer-by-layer films with nonconductive nanoparticles or polyions, {Au/Mb}n films showed much improved properties, such as smaller electron-transfer resistance (Rct) measured by EIS with Fe(CN)3-/4- redox probe, higher maximum surface concentration of electroactive Mb (Gamma*max), and better electrocatalytic activity toward reduction of O2 and H2O2, mainly because of the good conductivity of Au nanoparticles. Hydrogen Peroxide 369-373 myoglobin Homo sapiens 94-96 16471801-4 2006 Compared with other Mb layer-by-layer films with nonconductive nanoparticles or polyions, {Au/Mb}n films showed much improved properties, such as smaller electron-transfer resistance (Rct) measured by EIS with Fe(CN)3-/4- redox probe, higher maximum surface concentration of electroactive Mb (Gamma*max), and better electrocatalytic activity toward reduction of O2 and H2O2, mainly because of the good conductivity of Au nanoparticles. Hydrogen Peroxide 369-373 myoglobin Homo sapiens 94-96 15741099-1 2005 A new method has been developed for the determination of myoglobin (Mb) based on its enzymatic activity for the oxidation of o-phenylenediamine (OPDA) with hydrogen peroxide. Hydrogen Peroxide 156-173 myoglobin Homo sapiens 57-66 15741099-1 2005 A new method has been developed for the determination of myoglobin (Mb) based on its enzymatic activity for the oxidation of o-phenylenediamine (OPDA) with hydrogen peroxide. Hydrogen Peroxide 156-173 myoglobin Homo sapiens 68-70