PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27343172-3 2016 At low thiocyanate concentration and in the presence of hydrogen peroxide the observed reaction sequence is Compound I ferric MPO Compound II MPO-cyanide complex, whereas at high thiocyanate concentrations and in the absence of H2O2 the only observed transition is Compound I ferric MPO. Cyanides 146-153 myeloperoxidase Homo sapiens 126-129 27343172-3 2016 At low thiocyanate concentration and in the presence of hydrogen peroxide the observed reaction sequence is Compound I ferric MPO Compound II MPO-cyanide complex, whereas at high thiocyanate concentrations and in the absence of H2O2 the only observed transition is Compound I ferric MPO. Cyanides 146-153 myeloperoxidase Homo sapiens 142-145 27343172-3 2016 At low thiocyanate concentration and in the presence of hydrogen peroxide the observed reaction sequence is Compound I ferric MPO Compound II MPO-cyanide complex, whereas at high thiocyanate concentrations and in the absence of H2O2 the only observed transition is Compound I ferric MPO. Cyanides 146-153 myeloperoxidase Homo sapiens 142-145 27343172-4 2016 The reaction of ferric MPO with hypothiocyanite directly forms the MPO-cyanide complex, whereas a transient product derived from the reaction between hypothiocyanite and hydrogen peroxide is demonstrated to mediate the conversion of ferric MPO to Compound II. Cyanides 71-78 myeloperoxidase Homo sapiens 23-26 27343172-4 2016 The reaction of ferric MPO with hypothiocyanite directly forms the MPO-cyanide complex, whereas a transient product derived from the reaction between hypothiocyanite and hydrogen peroxide is demonstrated to mediate the conversion of ferric MPO to Compound II. Cyanides 71-78 myeloperoxidase Homo sapiens 67-70 27343172-4 2016 The reaction of ferric MPO with hypothiocyanite directly forms the MPO-cyanide complex, whereas a transient product derived from the reaction between hypothiocyanite and hydrogen peroxide is demonstrated to mediate the conversion of ferric MPO to Compound II. Cyanides 71-78 myeloperoxidase Homo sapiens 67-70 19705807-1 2009 The chief sources of cyanide (CN(-)) in humans are tobacco and occupationally derived smoke, inflammation [vis-a-vis myeloperoxidase (MPO)-induced chlorination of glycine], and microbial cyanogenesis (including Pseudomonas aeruginosa infection of the cystic fibrosis lung). Cyanides 21-28 myeloperoxidase Homo sapiens 134-137 25614581-0 2016 In vitro activation of dibromoacetonitrile to cyanide by myeloperoxidase. Cyanides 46-53 myeloperoxidase Homo sapiens 57-72 25614581-2 2016 This study aimed at investigating the ability of myeloperoxidase (MPO) to oxidize DBAN to cyanide (CN-) in vitro Detection of CN- served as a marker for the possible generation of free radical intermediates implicated in DBAN-induced toxicity. Cyanides 90-97 myeloperoxidase Homo sapiens 49-64 25614581-2 2016 This study aimed at investigating the ability of myeloperoxidase (MPO) to oxidize DBAN to cyanide (CN-) in vitro Detection of CN- served as a marker for the possible generation of free radical intermediates implicated in DBAN-induced toxicity. Cyanides 90-97 myeloperoxidase Homo sapiens 66-69 25614581-2 2016 This study aimed at investigating the ability of myeloperoxidase (MPO) to oxidize DBAN to cyanide (CN-) in vitro Detection of CN- served as a marker for the possible generation of free radical intermediates implicated in DBAN-induced toxicity. Cyanides 99-102 myeloperoxidase Homo sapiens 49-64 25614581-2 2016 This study aimed at investigating the ability of myeloperoxidase (MPO) to oxidize DBAN to cyanide (CN-) in vitro Detection of CN- served as a marker for the possible generation of free radical intermediates implicated in DBAN-induced toxicity. Cyanides 99-102 myeloperoxidase Homo sapiens 66-69 17042493-3 2006 The E(o)" values for free and cyanide-bound MPO (5 and -37 mV, respectively, at 25 degrees C and pH 7.0) are significantly higher than those of other heme peroxidases. Cyanides 30-37 myeloperoxidase Homo sapiens 44-47 17359937-5 2007 Compared with wild-type recombinant MPO the cyanide association rate with ferric Met243Val was significantly enhanced as were also the calculated apparent bimolecular compound I reduction rates by iodide (>10(8) M(-1)s(-1)) and thiocyanate (>10(8) M(-1)s(-1)). Cyanides 44-51 myeloperoxidase Homo sapiens 36-39 17042493-6 2006 This peculiar behavior is discussed with respect to the MPO-typical covalent heme to protein linkages as well as to the published structures of ferric MPO and its cyanide complex and the recently published structure of lactoperoxidase as well as the physiological role of MPO in bacterial killing. Cyanides 163-170 myeloperoxidase Homo sapiens 151-154 17042493-6 2006 This peculiar behavior is discussed with respect to the MPO-typical covalent heme to protein linkages as well as to the published structures of ferric MPO and its cyanide complex and the recently published structure of lactoperoxidase as well as the physiological role of MPO in bacterial killing. Cyanides 163-170 myeloperoxidase Homo sapiens 151-154 14687762-0 2004 Myeloperoxidase-catalyzed oxidation of chloroacetonitrile to cyanide. Cyanides 61-68 myeloperoxidase Homo sapiens 0-15 15203186-10 2004 MPO-mediated lipid oxidation was inhibited by heme poisons (azide, cyanide) and catalase. Cyanides 67-74 myeloperoxidase Homo sapiens 0-3 16288970-4 2006 Based on the published crystal structures of free MPO and its complexes with cyanide, bromide and thiocyanate as well as on sequence analysis and modeling, we critically discuss structure-function relationships. Cyanides 77-84 myeloperoxidase Homo sapiens 50-53 14687762-3 2004 The present work provides an evidence for CAN activation to cyanide (CN-) by myeloperoxidase (MPO)/hydrogen peroxide (H2O2)/chloride (Cl-) system in vitro. Cyanides 60-67 myeloperoxidase Homo sapiens 77-92 14687762-3 2004 The present work provides an evidence for CAN activation to cyanide (CN-) by myeloperoxidase (MPO)/hydrogen peroxide (H2O2)/chloride (Cl-) system in vitro. Cyanides 60-67 myeloperoxidase Homo sapiens 94-97 11258981-6 2001 The myeloperoxidase-catalyzed reaction with 0.3 mM NO(2)(-) was completely inhibited by 1 mM cyanide, and not effected by 100 mM chloride with or without 1 mM taurine. Cyanides 93-100 myeloperoxidase Homo sapiens 4-19 11705390-0 2001 Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution. Cyanides 38-45 myeloperoxidase Homo sapiens 6-21 11705390-1 2001 The 1.9 A X-ray crystal structure of human myeloperoxidase complexed with cyanide (R = 0.175, R(free) = 0.215) indicates that cyanide binds to the heme iron with a bent Fe-C-N angle of approximately 157 degrees, and binding is accompanied by movement of the iron atom by 0.2 A into the porphyrin plane. Cyanides 74-81 myeloperoxidase Homo sapiens 43-58 11705390-1 2001 The 1.9 A X-ray crystal structure of human myeloperoxidase complexed with cyanide (R = 0.175, R(free) = 0.215) indicates that cyanide binds to the heme iron with a bent Fe-C-N angle of approximately 157 degrees, and binding is accompanied by movement of the iron atom by 0.2 A into the porphyrin plane. Cyanides 126-133 myeloperoxidase Homo sapiens 43-58 11705390-5 2001 The 1.9 A structures of the complexes formed by bromide (R = 0.215, R(free) = 0.270) and thiocyanate (R = 0.198, R(free) = 0.224) with the cyanide complex of myeloperoxidase show how the presence of bound cyanide alters the binding site for bromide in the distal heme cavity, while having little effect on thiocyanate binding. Cyanides 139-146 myeloperoxidase Homo sapiens 158-173 11705390-5 2001 The 1.9 A structures of the complexes formed by bromide (R = 0.215, R(free) = 0.270) and thiocyanate (R = 0.198, R(free) = 0.224) with the cyanide complex of myeloperoxidase show how the presence of bound cyanide alters the binding site for bromide in the distal heme cavity, while having little effect on thiocyanate binding. Cyanides 205-212 myeloperoxidase Homo sapiens 158-173 10462537-9 1999 )radicals is completely blocked by myeloperoxidase inhibitors, cyanide and azide. Cyanides 77-84 myeloperoxidase Homo sapiens 49-64 3038442-2 1987 Catalase, azide, cyanide and three aminoacids employed as quenchers of ClO, significantly inhibited this nonspecific cytotoxicity (NSC), suggesting an important role for the myeloperoxidase (MPO) system. Cyanides 17-24 myeloperoxidase Homo sapiens 174-189 8399138-5 1993 On the basis of a previous normal-mode analysis of the cyanoferric adduct of myeloperoxidase, a bent Fe-C-N linkage is suggested for the cyanide adduct of lactoperoxidase. Cyanides 137-144 myeloperoxidase Homo sapiens 77-92 1316115-4 1992 Degradation of MeHg and EtHg with the myeloperoxidase (MPO)-H2O2-chloride system was inhibited by MPO inhibitors (cyanide and azide), catalase, hypochlorous acid (HOCI) scavengers (glycine, alanine, serine and taurine), 1,4-diazabicyclo[2,2,2]octane and 2,5-dimethylfuran, but not by hydroxyl radical scavengers (ethanol and mannitol). Cyanides 114-121 myeloperoxidase Homo sapiens 38-53 1316115-4 1992 Degradation of MeHg and EtHg with the myeloperoxidase (MPO)-H2O2-chloride system was inhibited by MPO inhibitors (cyanide and azide), catalase, hypochlorous acid (HOCI) scavengers (glycine, alanine, serine and taurine), 1,4-diazabicyclo[2,2,2]octane and 2,5-dimethylfuran, but not by hydroxyl radical scavengers (ethanol and mannitol). Cyanides 114-121 myeloperoxidase Homo sapiens 55-58 1316115-4 1992 Degradation of MeHg and EtHg with the myeloperoxidase (MPO)-H2O2-chloride system was inhibited by MPO inhibitors (cyanide and azide), catalase, hypochlorous acid (HOCI) scavengers (glycine, alanine, serine and taurine), 1,4-diazabicyclo[2,2,2]octane and 2,5-dimethylfuran, but not by hydroxyl radical scavengers (ethanol and mannitol). Cyanides 114-121 myeloperoxidase Homo sapiens 98-101 1847831-0 1991 Interaction of halides with the cyanide complex of myeloperoxidase: a model for substrate binding to compound I. EPR spectra of the low-spin cyanide complex of myeloperoxidase have been measured in the absence and presence of halide substrates; chloride, bromide and iodide. Cyanides 32-39 myeloperoxidase Homo sapiens 51-66 1847831-0 1991 Interaction of halides with the cyanide complex of myeloperoxidase: a model for substrate binding to compound I. EPR spectra of the low-spin cyanide complex of myeloperoxidase have been measured in the absence and presence of halide substrates; chloride, bromide and iodide. Cyanides 141-148 myeloperoxidase Homo sapiens 51-66 1847831-0 1991 Interaction of halides with the cyanide complex of myeloperoxidase: a model for substrate binding to compound I. EPR spectra of the low-spin cyanide complex of myeloperoxidase have been measured in the absence and presence of halide substrates; chloride, bromide and iodide. Cyanides 141-148 myeloperoxidase Homo sapiens 160-175 3011897-3 1986 Detoxification required each component of the myeloperoxidase system and was prevented by the addition of agents that inhibit heme enzymes (azide, cyanide) or degrade H2O2 (catalase). Cyanides 147-154 myeloperoxidase Homo sapiens 46-61 6331509-0 1984 A kinetic study of the reaction between human myeloperoxidase, hydroperoxides and cyanide. Cyanides 82-89 myeloperoxidase Homo sapiens 46-61 6092276-8 1984 The NADP formation associated with a dense granule fraction observed previously in our laboratory was probably due to a cyanide-stimulated oxidation of NADPH by myeloperoxidase. Cyanides 120-127 myeloperoxidase Homo sapiens 161-176 2981925-12 1985 The addition of cyanide at various times interrupted lysis at once, indicating a requirement for ongoing myeloperoxidase-dependent reactions. Cyanides 16-23 myeloperoxidase Homo sapiens 105-120 6090506-3 1984 Inactivation of MPO with heat or with cyanide ion prevented light production. Cyanides 38-45 myeloperoxidase Homo sapiens 16-19 6331509-8 1984 The pH-dependence of the dissociation constant of the myeloperoxidase-chloride complex obtained from the spectral changes induced by chloride is the same as observed in the inhibition by chloride of the binding of cyanide. Cyanides 214-221 myeloperoxidase Homo sapiens 54-69 6331509-6 1984 The binding of cyanide to myeloperoxidase (k1 = (1.30 +/- 0.05) X 10(6) M-1 X s-1) is also regulated by an acid/base group with a pKa of 4.00 +/- 0.05 as is the case with hydrogen peroxide; also, only the protonated uncharged form of cyanide reacts with the enzyme. Cyanides 15-22 myeloperoxidase Homo sapiens 26-41 6331509-6 1984 The binding of cyanide to myeloperoxidase (k1 = (1.30 +/- 0.05) X 10(6) M-1 X s-1) is also regulated by an acid/base group with a pKa of 4.00 +/- 0.05 as is the case with hydrogen peroxide; also, only the protonated uncharged form of cyanide reacts with the enzyme. Cyanides 234-241 myeloperoxidase Homo sapiens 26-41 6331509-7 1984 From their effects on the binding of cyanide to the enzyme it is concluded that chloride and thiocyanate bind to myeloperoxidase only when the acid/base group is protonated. Cyanides 37-44 myeloperoxidase Homo sapiens 113-128 6292103-9 1982 Damage to hyphae by the myeloperoxidase system was inhibited by azide, cyanide, catalase, histidine, and tryptophan, but not by superoxide dismutase, dimethyl sulfoxide, or mannitol. Cyanides 71-78 myeloperoxidase Homo sapiens 24-39 6300255-2 1983 Inhibition by anaerobiosis, azide, cyanide, halide-free conditions, catalase, histidine, and tryptophan suggested mediation of hyphal damage primarily through the myeloperoxidase system. Cyanides 35-42 myeloperoxidase Homo sapiens 163-178 6267057-5 1981 In a cell-free system, the fluorescence of 3,3"-dipropylthiodicarbocyanine, but not that of 3,3"-dipentyloxadicarbocyanine, was rapidly eliminated by myeloperoxidase in the presence of hydrogen peroxide and a halide; this loss of fluorescence was inhibited by azide, cyanide, or catalase. Cyanides 267-274 myeloperoxidase Homo sapiens 150-165 6271809-10 1981 This conclusion was based on the kinetics and dose-response relationships for the effects of azide and cyanide on H2O2 release and on the activities of catalase and myeloperoxidase. Cyanides 103-110 myeloperoxidase Homo sapiens 165-180 6162845-3 1981 Inactivation was rapid (10 to 20 s); required active myeloperoxidase, micromolar concentrations of H2O2 (or glucose oxidase as a peroxide generator), and a halide cofactor (Cl- or I-); and was blocked by azide, cyanide, and catalase. Cyanides 211-218 myeloperoxidase Homo sapiens 53-68 4988715-1 1970 Azide and, to a lesser extent, cyanide inhibit the microbicidal activity of myeloperoxidase and of intact normal leukocytes, but they have little or no effect on peroxidase-negative leukocytes. Cyanides 31-38 myeloperoxidase Homo sapiens 76-91 6253528-10 1980 In the case of PMA-stimulated polymorphonuclear leukocytes or monocytes, extracellular myeloperoxidase may have also played a role in alpha(1)-Pi inactivation since serum EIC was partly protected by azide, cyanide, or the depletion of extracellular chloride. Cyanides 206-213 myeloperoxidase Homo sapiens 87-102 6246992-6 1980 The myeloperoxidase inhibitor cyanide did not reduce red blood destruction, while azide consistently impaired cytolysis. Cyanides 30-37 myeloperoxidase Homo sapiens 4-19 6244265-7 1980 When hydrazine was added to cyanide complex I of myeloperoxidase the complex was converted to the hydrazine-enzyme compound. Cyanides 28-35 myeloperoxidase Homo sapiens 49-64 6244265-8 1980 Myeloperoxidase reacted with bisulfite to form a compound with an absorption spectrum similar to that of cyanide complex I. Cyanides 105-112 myeloperoxidase Homo sapiens 0-15 6244265-9 1980 Borohydride-treated myeloperoxidase formed only one cyanide complex, while the native enzyme formed two different cyanide complexes, I (Kd = 0.3 muM) and II (approximate Kd = 0.1 mM). Cyanides 52-59 myeloperoxidase Homo sapiens 20-35 6244265-9 1980 Borohydride-treated myeloperoxidase formed only one cyanide complex, while the native enzyme formed two different cyanide complexes, I (Kd = 0.3 muM) and II (approximate Kd = 0.1 mM). Cyanides 114-121 myeloperoxidase Homo sapiens 20-35 6244265-10 1980 The EPR spectrum indicated that cyanide complex I of myeloperoxidase still contained high-spin heme. Cyanides 32-39 myeloperoxidase Homo sapiens 53-68 6244265-11 1980 The results suggested that cyanide complex I and the bisulfite compound of myeloperoxidase were adducts between the nucleophilic reagents and the formyl group of myeloperoxidase heme. Cyanides 27-34 myeloperoxidase Homo sapiens 75-90 6244265-11 1980 The results suggested that cyanide complex I and the bisulfite compound of myeloperoxidase were adducts between the nucleophilic reagents and the formyl group of myeloperoxidase heme. Cyanides 27-34 myeloperoxidase Homo sapiens 162-177 6244567-7 1980 The myeloperoxidase inhibitor cyanide enhanced erythrocyte destruction, whereas azide reduced it modestly. Cyanides 30-37 myeloperoxidase Homo sapiens 4-19 203651-4 1978 Further, inhibition of ethylene generation by azide and cyanide suggests that OH generation in granulocytes may be linked to myeloperoxidase. Cyanides 56-63 myeloperoxidase Homo sapiens 125-140 5116211-3 1971 Azide and cyanide increased glucose C-1 oxidation by normal leukocytes but had little or no effect on myeloperoxidase-deficient leukocytes suggesting that these agents normally stimulate glucose C-1 oxidation, in part, by inhibition of myeloperoxidase. Cyanides 10-17 myeloperoxidase Homo sapiens 236-251 36154-5 1979 Chloride competed with cyanide for binding at the active site of myeloperoxidase. Cyanides 23-30 myeloperoxidase Homo sapiens 65-80 176720-4 1976 Since hexose monophosphate shunt activity was enhanced and azide and cyanide inhibited the intracellular killing of E. coli only moderately, the patient"s granulocytes may possess azide- and cyanide-resistant, MPO-independant microbicidal systems coupled to the oxidative metabolism. Cyanides 191-198 myeloperoxidase Homo sapiens 210-213 170101-6 1975 Chlorination in neutrophils is inhibited by the iodide and myeloperoxidase inhibitors azide and cyanide. Cyanides 96-103 myeloperoxidase Homo sapiens 59-74 31383327-2 2019 Conversion of plant derived thiocyanates into cyanide and isocyanic acid occurs by the activity of neutrophil-derived enzyme myeloperoxidase. Cyanides 46-53 myeloperoxidase Homo sapiens 125-140 29496995-0 2018 Myeloperoxidase-catalyzed oxidation of cyanide to cyanate: A potential carbamylation route involved in the formation of atherosclerotic plaques? Cyanides 39-46 myeloperoxidase Homo sapiens 0-15 29496995-3 2018 This work demonstrates that the heme protein myeloperoxidase (MPO), which is secreted at high concentrations at inflammatory sites from stimulated neutrophils and monocytes, is able to catalyze the two-electron oxidation of cyanide to cyanate and promote the carbamylation of taurine, lysine, and low-density lipoproteins. Cyanides 224-231 myeloperoxidase Homo sapiens 45-60 29496995-3 2018 This work demonstrates that the heme protein myeloperoxidase (MPO), which is secreted at high concentrations at inflammatory sites from stimulated neutrophils and monocytes, is able to catalyze the two-electron oxidation of cyanide to cyanate and promote the carbamylation of taurine, lysine, and low-density lipoproteins. Cyanides 224-231 myeloperoxidase Homo sapiens 62-65 29496995-5 2018 Moreover, we present two further pathways of carbamylation that involve reaction products of MPO, namely oxidation of cyanide by hypochlorous acid and reaction of thiocyanate with chloramines. Cyanides 118-125 myeloperoxidase Homo sapiens 93-96 29496995-6 2018 Finally, using an in vivo approach with mice on a high-fat diet and carrying the human MPO gene, we found that during chronic exposure to cyanide, mimicking exposure to pollution and smoking, MPO promotes protein-bound accumulation of carbamyllysine (homocitrulline) in atheroma plaque, demonstrating a link between cyanide exposure and atheroma. Cyanides 138-145 myeloperoxidase Homo sapiens 87-90 29496995-6 2018 Finally, using an in vivo approach with mice on a high-fat diet and carrying the human MPO gene, we found that during chronic exposure to cyanide, mimicking exposure to pollution and smoking, MPO promotes protein-bound accumulation of carbamyllysine (homocitrulline) in atheroma plaque, demonstrating a link between cyanide exposure and atheroma. Cyanides 138-145 myeloperoxidase Homo sapiens 192-195 29496995-6 2018 Finally, using an in vivo approach with mice on a high-fat diet and carrying the human MPO gene, we found that during chronic exposure to cyanide, mimicking exposure to pollution and smoking, MPO promotes protein-bound accumulation of carbamyllysine (homocitrulline) in atheroma plaque, demonstrating a link between cyanide exposure and atheroma. Cyanides 316-323 myeloperoxidase Homo sapiens 87-90 29496995-6 2018 Finally, using an in vivo approach with mice on a high-fat diet and carrying the human MPO gene, we found that during chronic exposure to cyanide, mimicking exposure to pollution and smoking, MPO promotes protein-bound accumulation of carbamyllysine (homocitrulline) in atheroma plaque, demonstrating a link between cyanide exposure and atheroma. Cyanides 316-323 myeloperoxidase Homo sapiens 192-195 29496995-7 2018 In summary, our findings indicate that cyanide is a substrate for MPO and suggest an additional pathway for in vivo cyanate formation and protein carbamylation that involves MPO either directly or via its reaction products hypochlorous acid or chloramines. Cyanides 39-46 myeloperoxidase Homo sapiens 66-69 29496995-7 2018 In summary, our findings indicate that cyanide is a substrate for MPO and suggest an additional pathway for in vivo cyanate formation and protein carbamylation that involves MPO either directly or via its reaction products hypochlorous acid or chloramines. Cyanides 39-46 myeloperoxidase Homo sapiens 174-177