PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10994872-1 2000 Myeloperoxidase is very susceptible to reducing radicals because the reduction potential of the ferric/ferrous redox couple is much higher compared with other peroxidases. Ferric enterobactin ion 96-102 myeloperoxidase Homo sapiens 0-15 15130787-4 2004 In the absence of dioxygen, ferrous MPO decays to ferric MPO (0.04 s(-1) at pH 8 versus 1.4 s(-1) at pH 5). Ferric enterobactin ion 50-56 myeloperoxidase Homo sapiens 36-39 15130787-4 2004 In the absence of dioxygen, ferrous MPO decays to ferric MPO (0.04 s(-1) at pH 8 versus 1.4 s(-1) at pH 5). Ferric enterobactin ion 50-56 myeloperoxidase Homo sapiens 57-60 15130787-8 2004 The rate constant of dioxygen dissociation from compound III is much higher than conversion of compound III to ferric MPO (which is not affected by the oxygen concentration). Ferric enterobactin ion 111-117 myeloperoxidase Homo sapiens 118-121 11068048-4 2000 At pH 7 and 15 degrees C, the rate constant of the reaction between 3-chloroperoxybenzoic acid and ferric MPO was similar to that with hydrogen peroxide (1.8x10(7) M(-1) s(-1) and 1.4x10(7) M(-1) s(-1), respectively). Ferric enterobactin ion 99-105 myeloperoxidase Homo sapiens 106-109 10681518-5 2000 NO binds to both ferric (Fe(III), the catalytically active species) and ferrous (Fe(II)) forms of MPO, generating stable low-spin six-coordinate complexes, MPO-Fe(III).NO and MPO-Fe(II).NO, respectively. Ferric enterobactin ion 17-23 myeloperoxidase Homo sapiens 98-101 10681518-5 2000 NO binds to both ferric (Fe(III), the catalytically active species) and ferrous (Fe(II)) forms of MPO, generating stable low-spin six-coordinate complexes, MPO-Fe(III).NO and MPO-Fe(II).NO, respectively. Ferric enterobactin ion 17-23 myeloperoxidase Homo sapiens 156-159 10681518-5 2000 NO binds to both ferric (Fe(III), the catalytically active species) and ferrous (Fe(II)) forms of MPO, generating stable low-spin six-coordinate complexes, MPO-Fe(III).NO and MPO-Fe(II).NO, respectively. Ferric enterobactin ion 17-23 myeloperoxidase Homo sapiens 156-159 9637000-2 1998 The modification caused a shift of the Soret band in the light absorption spectrum, from 430 nm to 418 nm in the case of myeloperoxidase (native ferric form), and from 412 nm to 406 nm in the case of lactoperoxidase (native ferric form). Ferric enterobactin ion 145-151 myeloperoxidase Homo sapiens 121-136 9637000-2 1998 The modification caused a shift of the Soret band in the light absorption spectrum, from 430 nm to 418 nm in the case of myeloperoxidase (native ferric form), and from 412 nm to 406 nm in the case of lactoperoxidase (native ferric form). Ferric enterobactin ion 224-230 myeloperoxidase Homo sapiens 121-136 7686874-13 1993 The conversion of compound II to ferric MPO by DFO optimized the enzymatic activity of neutrophils, and in the presence of monochlorodimedon (compound II promoting agent) we measured an increased HOCl production. Ferric enterobactin ion 33-39 myeloperoxidase Homo sapiens 40-43 2822673-5 1987 Myeloperoxidase compound I reacted with H2O2 and returned to the ferric state with concomitant evolution of an O2 molecule. Ferric enterobactin ion 65-71 myeloperoxidase Homo sapiens 0-15 27343172-2 2016 Oxidation of thiocyanate to hypothiocyanite mediated by the redox intermediate Compound I rapidly restores the ferric state of MPO. Ferric enterobactin ion 111-117 myeloperoxidase Homo sapiens 127-130 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. Ferric enterobactin ion 16-22 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. Ferric enterobactin ion 16-22 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. Ferric enterobactin ion 16-22 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. Ferric enterobactin ion 233-239 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. Ferric enterobactin ion 233-239 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. Ferric enterobactin ion 233-239 myeloperoxidase Homo sapiens 67-70 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. Ferric enterobactin ion 144-150 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. Ferric enterobactin ion 144-150 myeloperoxidase Homo sapiens 151-154 1333417-1 1992 EPR (electron paramagnetic resonance) and optical spectroscopy show that human neutrophil myeloperoxidase is converted from ferric high-spin to low-spin by the addition of nitrite. Ferric enterobactin ion 124-130 myeloperoxidase Homo sapiens 90-105 1656885-4 1991 The unprocessed recombinant protein displays the characteristic light absorption spectra of ferric mature MPO and exhibits its typical spectral changes in the presence of dithionite or hydrogen peroxide. Ferric enterobactin ion 92-98 myeloperoxidase Homo sapiens 106-109 2985447-1 1985 The resonance Raman spectra of ferric derivatives of myeloperoxidase at pH 8 show ligand-dependent differences. Ferric enterobactin ion 31-37 myeloperoxidase Homo sapiens 53-68