PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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. Nitrites 167-174 myoglobin Homo sapiens 24-26 15080699-1 2004 Previous investigations of nitrite and nitric oxide reduction by myoglobin in surfactant film modified electrodes characterized several distinct steps in the denitrification pathway, including isolation of a nitroxyl adduct similar to that proposed in the P450nor catalytic cycle. Nitrites 27-34 myoglobin Homo sapiens 65-74 15740057-1 2005 The effect of curing agents (salt, glucose, nitrate, nitrite, and ascorbic acid) on the binding of skeletal peptides (carnosine and anserine) and a sarcoplasmic protein (myoglobin) with key flavor compounds (hexanal, octanal, 2-pentanone, 2-methylbutanal, and 3-methylbutanal) has been studied by solid-phase microextraction (SPME). Nitrites 53-60 myoglobin Homo sapiens 170-179 15740057-6 2005 Finally, sodium chloride, glucose, and nitrite increased the interaction of myoglobin with hexanal, octanal, and methional. Nitrites 39-46 myoglobin Homo sapiens 76-85 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)(-). Nitrites 119-126 myoglobin Homo sapiens 16-18 16216040-0 2006 Easy oxidation and nitration of human myoglobin by nitrite and hydrogen peroxide. Nitrites 51-58 myoglobin Homo sapiens 38-47 16216040-1 2006 The modification of human myoglobin (HMb) by reaction with nitrite and hydrogen peroxide has been investigated. Nitrites 59-66 myoglobin Homo sapiens 26-35 15803717-5 2004 The immobilized Mb displays the features of a peroxidase and acts in an electrocatalytic manner in the reduction of oxygen, trichloroacetic acid (TCA), and nitrite. Nitrites 156-163 myoglobin Homo sapiens 16-18 11444837-4 2001 We found that myoglobin catalyzed the oxidation of nitrite and promoted the nitration of tyrosine. Nitrites 51-58 myoglobin Homo sapiens 14-23 18968594-7 2002 Oxygen, trichloroacetic acid (TCA) and nitrite were catalytically reduced by Mb-PAM film electrodes with significant lowering of overpotential. Nitrites 39-46 myoglobin Homo sapiens 77-79 11444837-5 2001 Both nitrite oxidation and tyrosine nitration were H(2)O(2)-dependent and required the formation of ferryl (Fe(+4)) myoglobin. Nitrites 5-12 myoglobin Homo sapiens 116-125 34313417-3 2021 Outside of the primary NOS-dependent biosynthetic pathway, other hemoproteins, including hemoglobin and myoglobin, generate NO via the reduction of nitrite. Nitrites 148-155 myoglobin Homo sapiens 104-113 11254342-6 2001 Mb could act as an enzyme-like catalyst in DHP-PDDA films as demonstrated by catalytic reduction of trichloroacetic acid, nitrite, and oxygen with a decrease in the electrode potentials required. Nitrites 122-129 myoglobin Homo sapiens 0-2 1194276-3 1975 The oxygen-binding function of myoglobin, in situ in muscle fiber bundles, was abolished by treatment with nitrite of hydroxylamine, which convert oxymyoglobin in situ to high spin ferric myoglobin, or with phenylhydrazine, which converts oxymyoglobin to denatured products, or with 2-hydroxyethylhydrazine, which appears to remove myoglobin from the muslce. Nitrites 107-114 myoglobin Homo sapiens 31-40 1194276-3 1975 The oxygen-binding function of myoglobin, in situ in muscle fiber bundles, was abolished by treatment with nitrite of hydroxylamine, which convert oxymyoglobin in situ to high spin ferric myoglobin, or with phenylhydrazine, which converts oxymyoglobin to denatured products, or with 2-hydroxyethylhydrazine, which appears to remove myoglobin from the muslce. Nitrites 107-114 myoglobin Homo sapiens 150-159 1194276-3 1975 The oxygen-binding function of myoglobin, in situ in muscle fiber bundles, was abolished by treatment with nitrite of hydroxylamine, which convert oxymyoglobin in situ to high spin ferric myoglobin, or with phenylhydrazine, which converts oxymyoglobin to denatured products, or with 2-hydroxyethylhydrazine, which appears to remove myoglobin from the muslce. Nitrites 107-114 myoglobin Homo sapiens 150-159 25722172-0 2015 Nitrite detection in meat products samples by square-wave voltammetry at a new single walled carbon naonotubes--myoglobin modified electrode. Nitrites 0-7 myoglobin Homo sapiens 112-121 32891753-0 2020 Myoglobin promotes nitrite-dependent mitochondrial S-NITROSATION to mediate cytoprotection after hypoxia/reoxygenation. Nitrites 19-26 myoglobin Homo sapiens 0-9 32891753-3 2020 Nitrite, an endogenous signaling molecule and dietary constituent, mediates potent cardioprotection after I/R and this effect relies on its interaction with both myoglobin and mitochondria. Nitrites 0-7 myoglobin Homo sapiens 162-171 32891753-4 2020 While independent mechanistic studies have demonstrated that nitrite-mediated cardioprotection requires the presence of myoglobin and the post-translational S-nitrosation of critical cysteine residues on mitochondrial complex I, it is unclear whether myoglobin directly catalyzes the S-nitrosation of complex I or whether mitochondrial-dependent nitrite reductase activity contributes to S-nitrosation. Nitrites 61-68 myoglobin Homo sapiens 120-129 32891753-5 2020 Herein, using purified myoglobin and isolated mitochondria, we characterize and directly compare the nitrite reductase activities of mitochondria and myoglobin and assess their contribution to mitochondrial S-nitrosation. Nitrites 101-108 myoglobin Homo sapiens 23-32 32891753-5 2020 Herein, using purified myoglobin and isolated mitochondria, we characterize and directly compare the nitrite reductase activities of mitochondria and myoglobin and assess their contribution to mitochondrial S-nitrosation. Nitrites 101-108 myoglobin Homo sapiens 150-159 32891753-7 2020 Further, deoxygenated myoglobin catalyzes the nitrite-dependent S-nitrosation of mitochondrial proteins. Nitrites 46-53 myoglobin Homo sapiens 22-31 32891753-9 2020 Using a Chinese Hamster Ovary cell model stably transfected with human myoglobin, we show that both myoglobin and mitochondrial complex I expression are required for nitrite-dependent attenuation of cell death after anoxia/reoxygenation. Nitrites 166-173 myoglobin Homo sapiens 71-80 32891753-9 2020 Using a Chinese Hamster Ovary cell model stably transfected with human myoglobin, we show that both myoglobin and mitochondrial complex I expression are required for nitrite-dependent attenuation of cell death after anoxia/reoxygenation. Nitrites 166-173 myoglobin Homo sapiens 100-109 32891753-10 2020 These data expand the understanding of myoglobin"s role both as a nitrite reductase to a mediator of S-nitrosation and as a regulator of mitochondrial function, and have implications for nitrite-mediated cardioprotection after I/R. Nitrites 66-73 myoglobin Homo sapiens 39-48 29955103-6 2018 After APP treatment, nitrite was produced in myoglobin solution that provided a positive environment for nitrimyoglobin formation. Nitrites 21-28 myoglobin Homo sapiens 45-54 27815981-0 2017 Nitrite coordination in myoglobin. Nitrites 0-7 myoglobin Homo sapiens 24-33 27815981-1 2017 The coordination of nitrite in myoglobin (Mb) has been characterized by resonance Raman spectroscopy and the frequencies of the nitrite bound to the heme Fe as well to the 2-vinyl have been computed by density functional theory (DFT) calculations. Nitrites 20-27 myoglobin Homo sapiens 31-40 27815981-1 2017 The coordination of nitrite in myoglobin (Mb) has been characterized by resonance Raman spectroscopy and the frequencies of the nitrite bound to the heme Fe as well to the 2-vinyl have been computed by density functional theory (DFT) calculations. Nitrites 128-135 myoglobin Homo sapiens 31-40 26544504-1 2016 Globins, such as hemoglobin (Hb) and myoglobin (Mb), have gained attention for their ability to reduce nitrite (NO2(-)) to nitric oxide (NO). Nitrites 103-110 myoglobin Homo sapiens 37-46 28873645-3 2018 The combined effect of pH (from 7.2 to 3.2) and myoglobin oxidation state was evaluated in the reaction of nitrite with heme iron, and the observed rate constants of the reactions were determined. Nitrites 107-114 myoglobin Homo sapiens 48-57 28458145-0 2017 Chlorite reactivity with myoglobin: Analogy with peroxide and nitrite chemistry? Nitrites 62-69 myoglobin Homo sapiens 25-34 28363495-2 2017 Production of NO through the reduction of endogenous myocardial nitrite by deoxygenated myoglobin has been shown to significantly reduce myocardial infarction damage and ischemic injury. Nitrites 64-71 myoglobin Homo sapiens 88-97 26172912-0 2015 Distal Histidine Modulates the Unusual O-Binding of Nitrite to Myoglobin: Evidence from the Quantum Chemical Analysis of EPR Parameters. Nitrites 52-59 myoglobin Homo sapiens 63-72 26172912-2 2015 In contrast to the commonly found N-binding motif of nitrite to iron in synthetic models, the less commonly observed O-binding of nitrite to myoglobin ( Copeland , D. M. ; Soares , A. S. ; West , A. H. ; Richter-Addo , G. B. J. Inorg. Nitrites 130-137 myoglobin Homo sapiens 141-150 26172912-8 2015 Given to the very similar active sites, there exists a controversy within the two powerful experimental techniques in identifying the coordination motif of nitrite to myoglobin, which is central to understanding the denitrification mechanism. Nitrites 156-163 myoglobin Homo sapiens 167-176 26172912-9 2015 Herein, we report the computation of spin Hamiltonian EPR parameters of different linkage isomers of nitrite bound myoglobin using wave function based "ab initio" and density functional theories to shed light on the binding motif of nitrite to ferric iron. Nitrites 101-108 myoglobin Homo sapiens 115-124 26172912-9 2015 Herein, we report the computation of spin Hamiltonian EPR parameters of different linkage isomers of nitrite bound myoglobin using wave function based "ab initio" and density functional theories to shed light on the binding motif of nitrite to ferric iron. Nitrites 233-240 myoglobin Homo sapiens 115-124 25955505-8 2015 An excellent electrocatalytic response of the immobilized Mb toward nitrite in the absence of electron transfer mediators was observed. Nitrites 68-75 myoglobin Homo sapiens 58-60 25722172-4 2015 The use of the sensor for the detection of nitrite ions in samples of meat products leads to comparable results with those obtained with the standard Griess spectrophotometric assay (ISO 2918/1975), proving the suitability of using immobilized myoglobin as electrocatalyst in the nitrite reduction process. Nitrites 43-50 myoglobin Homo sapiens 244-253 25722172-4 2015 The use of the sensor for the detection of nitrite ions in samples of meat products leads to comparable results with those obtained with the standard Griess spectrophotometric assay (ISO 2918/1975), proving the suitability of using immobilized myoglobin as electrocatalyst in the nitrite reduction process. Nitrites 280-287 myoglobin Homo sapiens 244-253 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. Nitrites 113-120 myoglobin Homo sapiens 0-2 22425779-4 2012 Under normoxia, oxygenated myoglobin can scavenge excessive nitric oxide, while under hypoxia, deoxygenated myoglobin can reduce nitrite, an oxidative product of nitric oxide, to bioactive nitric oxide. Nitrites 129-136 myoglobin Homo sapiens 27-36 25262340-0 2015 MWCNT-cysteamine-Nafion modified gold electrode based on myoglobin for determination of hydrogen peroxide and nitrite. Nitrites 110-117 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(-)). Nitrites 313-320 myoglobin Homo sapiens 118-127 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. Nitrites 31-38 myoglobin Homo sapiens 79-81 24211453-0 2014 Direct electrochemistry of myoglobin at reduced graphene oxide-multiwalled carbon nanotubes-platinum nanoparticles nanocomposite and biosensing towards hydrogen peroxide and nitrite. Nitrites 174-181 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(-)). Nitrites 281-288 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(-)). Nitrites 281-288 myoglobin Homo sapiens 197-206 23953980-0 2014 Myoglobin"s novel role in nitrite-induced hypoxic vasodilation. Nitrites 26-33 myoglobin Homo sapiens 0-9 23953980-4 2014 We have unraveled the heme-protein myoglobin in vascular smooth muscle cells as a major source of NO generation by reduction of endogenous nitrite under hypoxia. Nitrites 139-146 myoglobin Homo sapiens 35-44 22425779-4 2012 Under normoxia, oxygenated myoglobin can scavenge excessive nitric oxide, while under hypoxia, deoxygenated myoglobin can reduce nitrite, an oxidative product of nitric oxide, to bioactive nitric oxide. Nitrites 129-136 myoglobin Homo sapiens 108-117 22425779-5 2012 Myoglobin-driven nitrite reduction can protect the heart from ischemia and reperfusion injury. Nitrites 17-24 myoglobin Homo sapiens 0-9 22425779-9 2012 The results revealed that oxygenated human myoglobin reacts with nitrite-derived nitric oxide to form ferric myoglobin and that deoxygenated human myoglobin acts as a nitrite reductase in vitro and in situ. Nitrites 65-72 myoglobin Homo sapiens 43-52 22425779-9 2012 The results revealed that oxygenated human myoglobin reacts with nitrite-derived nitric oxide to form ferric myoglobin and that deoxygenated human myoglobin acts as a nitrite reductase in vitro and in situ. Nitrites 65-72 myoglobin Homo sapiens 109-118 22425779-9 2012 The results revealed that oxygenated human myoglobin reacts with nitrite-derived nitric oxide to form ferric myoglobin and that deoxygenated human myoglobin acts as a nitrite reductase in vitro and in situ. Nitrites 65-72 myoglobin Homo sapiens 109-118 22498469-1 2012 Gold dendrites (AuD) were synthesized with egg white as the soft template and a novel nitrite (NO(2)(-)) biosensor was fabricated by assembly of a myoglobin (Mb)-L-cysteamine (Cys)-AuD biological hybrid. Nitrites 86-93 myoglobin Homo sapiens 147-156 22498469-1 2012 Gold dendrites (AuD) were synthesized with egg white as the soft template and a novel nitrite (NO(2)(-)) biosensor was fabricated by assembly of a myoglobin (Mb)-L-cysteamine (Cys)-AuD biological hybrid. Nitrites 86-93 myoglobin Homo sapiens 158-160 17568573-2 2007 Nitrite reduction to NO may be catalyzed by hemoglobin, myoglobin or other metal-containing enzymes and occurs at increasing rates under conditions of physiologic hypoxia or ischemia. Nitrites 0-7 myoglobin Homo sapiens 56-65 20675542-4 2010 In addition, myoglobin may also protect the heart against reactive oxygen species (ROS), and, under hypoxic conditions, deoxygenated myoglobin is able to reduce nitrite to NO(*) leading to a downregulation of the cardiac energy status and to a decreased heart injury after reoxygenation. Nitrites 161-168 myoglobin Homo sapiens 13-22 20675542-4 2010 In addition, myoglobin may also protect the heart against reactive oxygen species (ROS), and, under hypoxic conditions, deoxygenated myoglobin is able to reduce nitrite to NO(*) leading to a downregulation of the cardiac energy status and to a decreased heart injury after reoxygenation. Nitrites 161-168 myoglobin Homo sapiens 133-142 17905436-0 2008 Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations. Nitrites 89-96 myoglobin Homo sapiens 56-65 17905436-2 2008 Hemoglobin (Hb) and myoglobin (Mb) convert, under certain conditions, nitrite to NO. Nitrites 70-77 myoglobin Homo sapiens 20-29 20568729-0 2010 Synchrotron X-ray-induced photoreduction of ferric myoglobin nitrite crystals gives the ferrous derivative with retention of the O-bonded nitrite ligand. Nitrites 61-68 myoglobin Homo sapiens 51-60 20568729-0 2010 Synchrotron X-ray-induced photoreduction of ferric myoglobin nitrite crystals gives the ferrous derivative with retention of the O-bonded nitrite ligand. Nitrites 138-145 myoglobin Homo sapiens 51-60 20568729-1 2010 Exposure of a single crystal of the nitrite adduct of ferric myoglobin (Mb) at 100 K to high-intensity synchrotron X-ray radiation resulted in changes in the UV-vis spectrum that can be attributed to reduction of the ferric compound to the ferrous derivative. Nitrites 36-43 myoglobin Homo sapiens 61-70 20568729-1 2010 Exposure of a single crystal of the nitrite adduct of ferric myoglobin (Mb) at 100 K to high-intensity synchrotron X-ray radiation resulted in changes in the UV-vis spectrum that can be attributed to reduction of the ferric compound to the ferrous derivative. Nitrites 36-43 myoglobin Homo sapiens 72-74 19836457-7 2010 Deoxygenated myoglobin reduces nitrite to bioactive NO(*). Nitrites 31-38 myoglobin Homo sapiens 13-22 19836457-10 2010 During myocardial reperfusion after ischemia, myoglobin - via nitrite - regulates respiration and cellular viability. Nitrites 62-69 myoglobin Homo sapiens 46-55 19836457-12 2010 The reaction between myoglobin and nitrite thus seems to play an imminent role in the regulation of cardiac function in physiology and pathophysiology. Nitrites 35-42 myoglobin Homo sapiens 21-30 22062097-5 2008 Nitrite added to a batter of meat is partially oxidized to nitrate by sequestering oxygen - thus it acts as an antioxidant - a part of nitrite is bound to myoglobin, forming the heat stable NO-myoglobin, a part is bound to proteins or other substances in meat. Nitrites 0-7 myoglobin Homo sapiens 155-164 22062097-5 2008 Nitrite added to a batter of meat is partially oxidized to nitrate by sequestering oxygen - thus it acts as an antioxidant - a part of nitrite is bound to myoglobin, forming the heat stable NO-myoglobin, a part is bound to proteins or other substances in meat. Nitrites 0-7 myoglobin Homo sapiens 193-202 22062097-5 2008 Nitrite added to a batter of meat is partially oxidized to nitrate by sequestering oxygen - thus it acts as an antioxidant - a part of nitrite is bound to myoglobin, forming the heat stable NO-myoglobin, a part is bound to proteins or other substances in meat. Nitrites 135-142 myoglobin Homo sapiens 155-164 22062097-5 2008 Nitrite added to a batter of meat is partially oxidized to nitrate by sequestering oxygen - thus it acts as an antioxidant - a part of nitrite is bound to myoglobin, forming the heat stable NO-myoglobin, a part is bound to proteins or other substances in meat. Nitrites 135-142 myoglobin Homo sapiens 193-202