PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2605311-2 1989 Reduction of the pyridoxylated HbAo in the oxygen-ligated form by sodium borohydride gives unacceptable levels of methemoglobin (i.e., greater than 10%). Oxygen 43-49 hemoglobin subunit gamma 2 Homo sapiens 114-127 2559883-3 1989 Nitrosylhemoglobin shows a characteristic electron spin resonance (ESR) signal due to an odd electron localized on the nitrogen atom of NO and reacts with oxygen to yield nitrate and methemoglobin, which is rapidly reduced by methemoglobin reductase in red cells. Oxygen 155-161 hemoglobin subunit gamma 2 Homo sapiens 183-196 2627576-4 1989 Under in vivo conditions of oxygen tension, reaction rates were oxyhemoglobin greater than deoxyhemoglobin greater than methemoglobin. Oxygen 28-34 hemoglobin subunit gamma 2 Homo sapiens 120-133 2648673-5 1989 Relatively low levels of methemoglobin could complicate concomitant carbon monoxide poisoning by additive or synergistic effects on oxygen binding and delivery. Oxygen 132-138 hemoglobin subunit gamma 2 Homo sapiens 25-38 2559883-3 1989 Nitrosylhemoglobin shows a characteristic electron spin resonance (ESR) signal due to an odd electron localized on the nitrogen atom of NO and reacts with oxygen to yield nitrate and methemoglobin, which is rapidly reduced by methemoglobin reductase in red cells. Oxygen 155-161 hemoglobin subunit gamma 2 Homo sapiens 226-239 3318547-7 1987 Methemoglobin and carbon monoxide shift the oxygen dissociation curve to the left, so that intoxication with both substances reduces both total oxygen capacity and oxygen delivery of the remaining hemoglobin able to bind oxygen. Oxygen 44-50 hemoglobin subunit gamma 2 Homo sapiens 0-13 3115772-4 1987 In the presence of oxygen, the speed of methemoglobin formation was three to four times faster in the hemolyzed and plasma-free samples than in whole blood. Oxygen 19-25 hemoglobin subunit gamma 2 Homo sapiens 40-53 3318547-7 1987 Methemoglobin and carbon monoxide shift the oxygen dissociation curve to the left, so that intoxication with both substances reduces both total oxygen capacity and oxygen delivery of the remaining hemoglobin able to bind oxygen. Oxygen 144-150 hemoglobin subunit gamma 2 Homo sapiens 0-13 3318547-7 1987 Methemoglobin and carbon monoxide shift the oxygen dissociation curve to the left, so that intoxication with both substances reduces both total oxygen capacity and oxygen delivery of the remaining hemoglobin able to bind oxygen. Oxygen 144-150 hemoglobin subunit gamma 2 Homo sapiens 0-13 3318547-7 1987 Methemoglobin and carbon monoxide shift the oxygen dissociation curve to the left, so that intoxication with both substances reduces both total oxygen capacity and oxygen delivery of the remaining hemoglobin able to bind oxygen. Oxygen 144-150 hemoglobin subunit gamma 2 Homo sapiens 0-13 4062295-4 1985 Reduction of methemoglobin is optimally observed under nitrogen since, in the presence of oxygen, reduced divicine undergoes autoxidation. Oxygen 90-96 hemoglobin subunit gamma 2 Homo sapiens 13-26 3624223-3 1987 The reduction of a methemoglobin-oxyhemoglobin mixture with an imposed potential causes the electrochemical reduction of oxygen, the conversion of oxyhemoglobin into deoxyhemoglobin, and a simultaneous transformation of part of the molecules into methemoglobin. Oxygen 121-127 hemoglobin subunit gamma 2 Homo sapiens 19-32 3624223-3 1987 The reduction of a methemoglobin-oxyhemoglobin mixture with an imposed potential causes the electrochemical reduction of oxygen, the conversion of oxyhemoglobin into deoxyhemoglobin, and a simultaneous transformation of part of the molecules into methemoglobin. Oxygen 121-127 hemoglobin subunit gamma 2 Homo sapiens 247-260 3624223-4 1987 When fixed oxygen has disappeared, reduction of methemoglobin takes place. Oxygen 11-17 hemoglobin subunit gamma 2 Homo sapiens 48-61 3816735-14 1986 Oxidation of the Fe2+ in hemoglobin to Fe3+ forms methemoglobin, which is incapable of carrying either O2 or CO2. Oxygen 103-105 hemoglobin subunit gamma 2 Homo sapiens 50-63 6885792-6 1983 The known inactivation of methemoglobin by phenylhydrazine is shown to depend on H2O2 but not oxygen. Oxygen 94-100 hemoglobin subunit gamma 2 Homo sapiens 26-39 4017990-2 1985 The amount of methemoglobin formed was determined by an anaerobic modification of the Evelyn-Malloy method; 59% of the total hemoglobin of whole blood was oxidized to methemoglobin in the first 15 min of the oxygen exposure and 78% of the total hemoglobin was oxidized after 120 min of oxygen exposure. Oxygen 208-214 hemoglobin subunit gamma 2 Homo sapiens 14-27 4017990-2 1985 The amount of methemoglobin formed was determined by an anaerobic modification of the Evelyn-Malloy method; 59% of the total hemoglobin of whole blood was oxidized to methemoglobin in the first 15 min of the oxygen exposure and 78% of the total hemoglobin was oxidized after 120 min of oxygen exposure. Oxygen 208-214 hemoglobin subunit gamma 2 Homo sapiens 167-180 4017990-2 1985 The amount of methemoglobin formed was determined by an anaerobic modification of the Evelyn-Malloy method; 59% of the total hemoglobin of whole blood was oxidized to methemoglobin in the first 15 min of the oxygen exposure and 78% of the total hemoglobin was oxidized after 120 min of oxygen exposure. Oxygen 286-292 hemoglobin subunit gamma 2 Homo sapiens 14-27 3988729-17 1985 It is necessary for maintenance of the oxygen transport function of the red cell for reductants such as the methemoglobin reductase system, glutathione, and ascorbate to be able to reduce metHb to deoxy-Hb. Oxygen 39-45 hemoglobin subunit gamma 2 Homo sapiens 108-121 3832865-0 1985 Oxygen permeability of methemoglobin solutions soaked in Millipore filters. Oxygen 0-6 hemoglobin subunit gamma 2 Homo sapiens 23-36 7315740-2 1981 Interlocking O2 absorption and sulfide depletion data indicate that both oxyhemoglobin and methemoglobin are effective catalytic agents. Oxygen 13-15 hemoglobin subunit gamma 2 Homo sapiens 91-104 6301495-0 1983 The production of activated oxygen species by an interaction of methemoglobin with ascorbate. Oxygen 28-34 hemoglobin subunit gamma 2 Homo sapiens 64-77 7159446-0 1982 Diffusion of oxygen in methemoglobin solutions. Oxygen 13-19 hemoglobin subunit gamma 2 Homo sapiens 23-36 7315740-4 1981 It has also been established that the formation of methemoglobin following nitrite administration occurs preferentially under oxygen poor conditions. Oxygen 126-132 hemoglobin subunit gamma 2 Homo sapiens 51-64 7400118-2 1980 The reduction of methemoglobin by the reconstituted enzyme system could be easily detected with flavin at the physiological concentration (e.g., 0.1-1.0 microM), and the rates obtained with 0.1 and 1.0 microM FMN were 0.19 and 2.2 nmol heme reduced per min per ml, respectively, in the absence of oxygen. Oxygen 297-303 hemoglobin subunit gamma 2 Homo sapiens 17-30 7202682-0 1981 Methemoglobin formation and reduction in relation to hemoglobin oxygen affinity. Oxygen 64-70 hemoglobin subunit gamma 2 Homo sapiens 0-13 7350931-0 1980 Methemoglobin reduction in red cells: effect of a high oxygen affinity hemoglobin. Oxygen 55-61 hemoglobin subunit gamma 2 Homo sapiens 0-13 6990915-0 1980 Abnormal hemoglobin-oxygen affinity and surgical hemotherapy. Oxygen 20-26 hemoglobin subunit gamma 2 Homo sapiens 0-19 6252740-5 1980 In case of matrix containing n-hexyl groups deoxyHb is oxidized by O2 to MetHb, instead of being oxygenated to HbO2. Oxygen 67-69 hemoglobin subunit gamma 2 Homo sapiens 73-78 7378040-0 1980 Abnormal hemoglobin oxygen affinity and the coronary circulation. Oxygen 20-26 hemoglobin subunit gamma 2 Homo sapiens 0-19 7350931-1 1980 Erythrocytes from heterozygous carriers of the high oxygen affinity mutant hemoglobin, Hb Wood, demonstrate lower rates of methemoglobin reduction than normal human red cells when incubated in the in vitro system of Beutler and Baluda. Oxygen 52-58 hemoglobin subunit gamma 2 Homo sapiens 123-136 662882-0 1978 Myocardial oxygen-supply during hemodilution with stroma-free hemoglobin and methemoglobin solutions. Oxygen 11-17 hemoglobin subunit gamma 2 Homo sapiens 77-90 25408-0 1978 Oxygen affinity of hemoglobins F and A partially oxidized to methemoglobin: influence of 2,3-diphosphoglycerate. Oxygen 0-6 hemoglobin subunit gamma 2 Homo sapiens 61-74 22547-6 1978 The kinetics of the ligation of O2 and CO were used to characterize the affinity states of the valence-hybrid and its parent methemoglobin. Oxygen 32-34 hemoglobin subunit gamma 2 Homo sapiens 125-138 864782-3 1977 Therefore, NO affects the oxygen transport function of hemoglobin, decreasing the oxygen supply to peripheral tissues, because of (1) simple diminution of the available hemoglobin by the tightly bound NO, (2) the high affinity of hemoglobin for oxygen, and (3) the inevitable formation of methemoglobin. Oxygen 26-32 hemoglobin subunit gamma 2 Homo sapiens 289-302 598384-0 1977 Heterogeneity in the kinetics of oxygen binding to partially reduced human methemoglobin. Oxygen 33-39 hemoglobin subunit gamma 2 Homo sapiens 75-88 967792-0 1976 [Influence of methemoglobin in the measurement of oxygen consumption of the whole blood using an AO-oximeter]. Oxygen 50-56 hemoglobin subunit gamma 2 Homo sapiens 14-27 974115-6 1976 We followed the reaction of the reduced proteins to yield the oxyderivatives and measured the rate constants of the oxygenation process k reduced methemoglobin + O2 = 2.6 +/- 0.6-10(7) M-1-S-1 and k myoglobin + O2 = 1.8 +/- 0.2-10(7) M-1-S-1, all the rate constants were measured at pH = 6.8, I = 0.004, T = 22 +/- 2 degrees C. The high rate constant for reduced methemoglobin indicates that one-site-reduced methemoglobin is probably in the R state, as predicted for methemoglobin from X-ray analysis. Oxygen 162-164 hemoglobin subunit gamma 2 Homo sapiens 146-159 974115-6 1976 We followed the reaction of the reduced proteins to yield the oxyderivatives and measured the rate constants of the oxygenation process k reduced methemoglobin + O2 = 2.6 +/- 0.6-10(7) M-1-S-1 and k myoglobin + O2 = 1.8 +/- 0.2-10(7) M-1-S-1, all the rate constants were measured at pH = 6.8, I = 0.004, T = 22 +/- 2 degrees C. The high rate constant for reduced methemoglobin indicates that one-site-reduced methemoglobin is probably in the R state, as predicted for methemoglobin from X-ray analysis. Oxygen 162-164 hemoglobin subunit gamma 2 Homo sapiens 363-376 974115-6 1976 We followed the reaction of the reduced proteins to yield the oxyderivatives and measured the rate constants of the oxygenation process k reduced methemoglobin + O2 = 2.6 +/- 0.6-10(7) M-1-S-1 and k myoglobin + O2 = 1.8 +/- 0.2-10(7) M-1-S-1, all the rate constants were measured at pH = 6.8, I = 0.004, T = 22 +/- 2 degrees C. The high rate constant for reduced methemoglobin indicates that one-site-reduced methemoglobin is probably in the R state, as predicted for methemoglobin from X-ray analysis. Oxygen 162-164 hemoglobin subunit gamma 2 Homo sapiens 363-376 974115-6 1976 We followed the reaction of the reduced proteins to yield the oxyderivatives and measured the rate constants of the oxygenation process k reduced methemoglobin + O2 = 2.6 +/- 0.6-10(7) M-1-S-1 and k myoglobin + O2 = 1.8 +/- 0.2-10(7) M-1-S-1, all the rate constants were measured at pH = 6.8, I = 0.004, T = 22 +/- 2 degrees C. The high rate constant for reduced methemoglobin indicates that one-site-reduced methemoglobin is probably in the R state, as predicted for methemoglobin from X-ray analysis. Oxygen 162-164 hemoglobin subunit gamma 2 Homo sapiens 363-376 974115-6 1976 We followed the reaction of the reduced proteins to yield the oxyderivatives and measured the rate constants of the oxygenation process k reduced methemoglobin + O2 = 2.6 +/- 0.6-10(7) M-1-S-1 and k myoglobin + O2 = 1.8 +/- 0.2-10(7) M-1-S-1, all the rate constants were measured at pH = 6.8, I = 0.004, T = 22 +/- 2 degrees C. The high rate constant for reduced methemoglobin indicates that one-site-reduced methemoglobin is probably in the R state, as predicted for methemoglobin from X-ray analysis. Oxygen 211-213 hemoglobin subunit gamma 2 Homo sapiens 146-159 5604707-0 1967 [On the effect of high oxygen and air pressure in experimental hypoxia evoked by acute poisoning due to methemoglobin-forming agents]. Oxygen 23-29 hemoglobin subunit gamma 2 Homo sapiens 104-117 163828-1 1975 Phenylhydrazine reacts with adult oxy- or methemoglobin in the presence of molecular oxygen to generate O2-. Oxygen 104-106 hemoglobin subunit gamma 2 Homo sapiens 42-55 4802071-2 1973 Oxygen partial pressure and methemoglobin formation during dialysis of preserved blood in the cellophane membrane artificial kidney with PD375 and oxygen insufflation and with added hydrogen peroxide]. Oxygen 147-153 hemoglobin subunit gamma 2 Homo sapiens 28-41 4396525-0 1970 [Influence of alpha and beta receptor blockaders upon oxygen consumption of methemoglobin containing erythrocytes]. Oxygen 54-60 hemoglobin subunit gamma 2 Homo sapiens 76-89 241510-1 1975 We report here the development of a new method that allows continuous determination of the oxygen dissociation curve for microsamples (600 mul) of whole blood under conditions of pH, pCO2, methemoglobin concentration, and 2,3-diphosphoglycerate content closely approaching those found in the circulatory system. Oxygen 91-97 hemoglobin subunit gamma 2 Homo sapiens 189-202 13906371-2 1962 The exchange of oxygen through the membrane was studied by means of oxygen-18, and it grossly exceeded that obtained with membranes containing methemoglobin or only water. Oxygen 16-22 hemoglobin subunit gamma 2 Homo sapiens 143-156 4379842-0 1965 [Methemoglobin formation by sulfonamides in a system containing liver homogenates, erythrocytes, NADPH and oxygen]. Oxygen 107-113 hemoglobin subunit gamma 2 Homo sapiens 1-14 19868522-1 1921 In the occasional cases of pneumonia which show a decrease in the oxygen capacity of the blood, the decrease is probably due to a formation of methemoglobin. Oxygen 66-72 hemoglobin subunit gamma 2 Homo sapiens 143-156 14937496-0 1952 [Diffusion constant of oxygen in methemoglobin solutions of different concentrations]. Oxygen 23-29 hemoglobin subunit gamma 2 Homo sapiens 33-46 19868989-6 1925 The equilibrium between hemoglobin and methemoglobin in a mixture of blood and pneumococcus cellular substances may be shifted in either direction at will by regulation of the oxygen tension. Oxygen 176-182 hemoglobin subunit gamma 2 Homo sapiens 39-52 18111542-0 1948 Intracorpuscular methemoglobin formation and its relation to the rate of oxygen release. Oxygen 73-79 hemoglobin subunit gamma 2 Homo sapiens 17-30 19871691-6 1947 Deoxygnated hemoglobin in the dry state was partly converted to methemoglobin by even momentary contact with oxygen. Oxygen 109-115 hemoglobin subunit gamma 2 Homo sapiens 64-77 33871764-1 2022 Almost since its introduction pulse oximetry was known to overestimate oxygen saturation in cases of carbon monoxide poisoning or elevated methemoglobin (metHb) levels. Oxygen 71-77 hemoglobin subunit gamma 2 Homo sapiens 139-152 33978488-6 2021 The most plausible cause for this finding is formation of methemoglobin, which increases the oxygen affinity and thus apparently compensates for the 2,3-BPG effect. Oxygen 93-99 hemoglobin subunit gamma 2 Homo sapiens 58-71 33611266-16 2021 Methemoglobinemia means the abnormally elevated level of methemoglobin in the blood, which is incapable of oxygen transport, accordingly it can cause significant tissue hypoxia, leading to severe or even life-threatening clinical symptoms. Oxygen 107-113 hemoglobin subunit gamma 2 Homo sapiens 57-70 33427354-6 2021 We successfully used NAD+ from the nanoreactors for the the continuous production of NAD+ to 1) sense glucose in an artificial glucose metabolism, and 2) to reduce the non-oxygen binding methemoglobin to oxygen-binding hemoglobin. Oxygen 172-178 hemoglobin subunit gamma 2 Homo sapiens 187-200 33427354-6 2021 We successfully used NAD+ from the nanoreactors for the the continuous production of NAD+ to 1) sense glucose in an artificial glucose metabolism, and 2) to reduce the non-oxygen binding methemoglobin to oxygen-binding hemoglobin. Oxygen 204-210 hemoglobin subunit gamma 2 Homo sapiens 187-200 33598944-5 2021 Death is a consequence of oxidation of hemoglobin ferrous (Fe+2 ) iron (Hb) to the ferric (Fe+3 ) form (methemoglobin, MetHb), causing a reduction in the oxygen-carrying capacity of the blood. Oxygen 154-160 hemoglobin subunit gamma 2 Homo sapiens 104-117 33380153-3 2020 Methemoglobin has reduced ability to release oxygen to tissues and thereby leads to tissue hypoxia. Oxygen 45-51 hemoglobin subunit gamma 2 Homo sapiens 0-13 33256027-1 2020 Methemoglobin (MetHb) is a hemoglobin (Hb) derivative with the heme iron in ferric state (Fe3+), unable to deliver oxygen. Oxygen 115-121 hemoglobin subunit gamma 2 Homo sapiens 0-13 33256027-1 2020 Methemoglobin (MetHb) is a hemoglobin (Hb) derivative with the heme iron in ferric state (Fe3+), unable to deliver oxygen. Oxygen 115-121 hemoglobin subunit gamma 2 Homo sapiens 15-20 33074043-1 2021 Sodium nitrite is a powerful oxidizing agent that causes hypotension and limits oxygen transport and delivery in the body through the formation of methemoglobin. Oxygen 80-86 hemoglobin subunit gamma 2 Homo sapiens 147-160 33578723-0 2021 Function of Hemoglobin-Based Oxygen Carriers: Determination of Methemoglobin Content by Spectral Extinction Measurements. Oxygen 29-35 hemoglobin subunit gamma 2 Homo sapiens 63-76 33583153-13 2021 Changes in methemoglobin concentration and tissue oxygen saturation are indicative of the temporary production of methemoglobin and severe hypoxemia during methemoglobinemia. Oxygen 50-56 hemoglobin subunit gamma 2 Homo sapiens 114-127 30016042-2 2018 Methemoglobinemia is a disorder that occurs when hemoglobin in the blood is oxidized to form methemoglobin, rendering it unable to transport oxygen. Oxygen 141-147 hemoglobin subunit gamma 2 Homo sapiens 93-106 32257839-2 2020 The derivative known as methemoglobin results from oxidation of hemoglobin and is pathologically relevant because it cannot transport oxygen. Oxygen 134-140 hemoglobin subunit gamma 2 Homo sapiens 24-37 31754421-1 2019 Methemoglobin (MetHb) is an oxidized form on hemoglobin, which is unable to bind oxygen and consequently carry it to the tissues. Oxygen 81-87 hemoglobin subunit gamma 2 Homo sapiens 0-13 31754421-1 2019 Methemoglobin (MetHb) is an oxidized form on hemoglobin, which is unable to bind oxygen and consequently carry it to the tissues. Oxygen 81-87 hemoglobin subunit gamma 2 Homo sapiens 15-20 31142197-4 2019 The primary outcome was to describe the relationship between Met-Hb and other indices of tissue oxygenation (venous saturation, estimated arteriovenous oxygen difference [Est AV-Diff], and lactate). Oxygen 96-102 hemoglobin subunit gamma 2 Homo sapiens 61-67 31142197-8 2019 Venous Met-Hb demonstrated a significant inverse relationship with venous oxygen saturation (R = -0.6; P < .001) and Hb (R = -0.3, P < .001) and a direct relationship with the Est AV-Diff (R = 0.3, P < .001). Oxygen 74-80 hemoglobin subunit gamma 2 Homo sapiens 7-13 32863537-4 2019 The RBC hemoglobin oxygen saturation determines the hemoglobin molecular magnetic susceptibility (diamagnetic when fully oxygenated, paramagnetic when fully deoxygenated or converted to methemoglobin). Oxygen 19-25 hemoglobin subunit gamma 2 Homo sapiens 186-199 30293223-3 2019 This is an unusual and potentially fatal condition in which hemoglobin is oxidized to methemoglobin (MHb), reducing the amount of oxygen that is released from hemoglobin, similar to carbon monoxide poisoning. Oxygen 130-136 hemoglobin subunit gamma 2 Homo sapiens 86-99 30293223-3 2019 This is an unusual and potentially fatal condition in which hemoglobin is oxidized to methemoglobin (MHb), reducing the amount of oxygen that is released from hemoglobin, similar to carbon monoxide poisoning. Oxygen 130-136 hemoglobin subunit gamma 2 Homo sapiens 101-104 28259531-8 2017 We present a case of unusually severe methemoglobinemia (82% methemoglobin) secondary to occupational exposure that failed to respond to several lines of management including methylene blue, red cell exchange, intravenous ascorbic acid, and hyperbaric oxygen. Oxygen 252-258 hemoglobin subunit gamma 2 Homo sapiens 38-51 28345492-2 2018 The drug has oxidizing potential and as an adverse effect, it can convert the ferrous form of iron in erythrocytes to its ferric form resulting in the formation of methemoglobin which makes the heme component incapable of carrying oxygen. Oxygen 231-237 hemoglobin subunit gamma 2 Homo sapiens 164-177 29185409-2 2017 The delivery of oxygen to tissues is impaired and cellular hypoxia develops with an increase in MetHb levels. Oxygen 16-22 hemoglobin subunit gamma 2 Homo sapiens 96-101 28838565-8 2017 While administering oxygen flowing at 15 L/min via a mask with a reservoir bag, blood tests revealed high methemoglobin (MetHb) levels at 59.6%. Oxygen 20-26 hemoglobin subunit gamma 2 Homo sapiens 106-119 28838565-8 2017 While administering oxygen flowing at 15 L/min via a mask with a reservoir bag, blood tests revealed high methemoglobin (MetHb) levels at 59.6%. Oxygen 20-26 hemoglobin subunit gamma 2 Homo sapiens 121-126 28912721-9 2017 Results: Conditions of hyperglycaemia are characterized by a low affinity of hemoglobin to oxygen, which is manifested as a parallel decrease in the content of hemoglobin oxyform and the growth of deoxyform, methemoglobin and membrane-bound hemoglobin. Oxygen 91-97 hemoglobin subunit gamma 2 Homo sapiens 208-221 28230974-1 2017 The magnetic characteristics of hemoglobin (Hb) changes with the binding of dioxygen (O2) to the heme prosthetic groups of the globin chains: from paramagnetic ferrous Hb to diamagnetic ferrous oxyhemoglobin (oxyHb) with reversibly bound O2, or paramagnetic ferric methemoglobin (metHb). Oxygen 76-84 hemoglobin subunit gamma 2 Homo sapiens 265-278 28082013-6 2017 The increase of methemoglobin up to 13.8% was accompanied by hypoxemia and cyanosis, necessitating additional inspired oxygen and CPAP ventilation. Oxygen 119-125 hemoglobin subunit gamma 2 Homo sapiens 16-29 28230974-1 2017 The magnetic characteristics of hemoglobin (Hb) changes with the binding of dioxygen (O2) to the heme prosthetic groups of the globin chains: from paramagnetic ferrous Hb to diamagnetic ferrous oxyhemoglobin (oxyHb) with reversibly bound O2, or paramagnetic ferric methemoglobin (metHb). Oxygen 86-88 hemoglobin subunit gamma 2 Homo sapiens 265-278 28248201-3 2017 Nitric oxide (NO) is inactivated by cell-free hemoglobin in a dioxygenation reaction that also oxidizes hemoglobin to methemoglobin, a non-oxygen-binding form of hemoglobin that readily loses heme. Oxygen 64-70 hemoglobin subunit gamma 2 Homo sapiens 118-131 27747692-5 2016 The patient was treated with oxygen administration, but methemoglobin concentration was still 45 % 1 h later. Oxygen 29-35 hemoglobin subunit gamma 2 Homo sapiens 56-69 25617395-1 2015 Methemoglobin (MetHb) is a form of hemoglobin in which heme iron is oxidized and unable to bind oxygen; its normal basal production is counteracted by an efficient MetHb-reduction pathway. Oxygen 96-102 hemoglobin subunit gamma 2 Homo sapiens 0-13 27814710-1 2016 BACKGROUND: Exposure of red blood cells to oxidants increases production of methemoglobin (MHb) resulting in impaired oxygen delivery to tissues. Oxygen 118-124 hemoglobin subunit gamma 2 Homo sapiens 76-89 27814710-1 2016 BACKGROUND: Exposure of red blood cells to oxidants increases production of methemoglobin (MHb) resulting in impaired oxygen delivery to tissues. Oxygen 118-124 hemoglobin subunit gamma 2 Homo sapiens 91-94 25885573-7 2015 Since observed tendencies are suggestive of a possible genetic adaptation to hypoxia of the Chilean Aymara, we discuss briefly preliminary evidence related to fetal oxygen transport, particularly polymorphisms in the promoters of the HBG1 and HBG2 genes that are modulators of HbF synthesis, obtained in this ethnic group. Oxygen 165-171 hemoglobin subunit gamma 2 Homo sapiens 243-247 25617395-1 2015 Methemoglobin (MetHb) is a form of hemoglobin in which heme iron is oxidized and unable to bind oxygen; its normal basal production is counteracted by an efficient MetHb-reduction pathway. Oxygen 96-102 hemoglobin subunit gamma 2 Homo sapiens 15-20 25617395-7 2015 This case emphasizes causes of methemoglobinemia and differences among analytical methods used to measure oxygen status when MetHb is present. Oxygen 106-112 hemoglobin subunit gamma 2 Homo sapiens 125-130 27366424-3 2014 Methemoglobinemia is a serious clinical condition, associated with increased blood methemoglobin levels characterized by clinical signs, such as cyanosis and hypoxia due to lack of oxygen-carrying capacity. Oxygen 181-187 hemoglobin subunit gamma 2 Homo sapiens 83-96 24342540-1 2014 Hemoglobin (Hb) as an important iron-containing oxygen-transport protein is easily oxidized to the ferric met-form, methemoglobin (metHb), and loses the capacity of binding oxygen during storage. Oxygen 48-54 hemoglobin subunit gamma 2 Homo sapiens 116-129 24342540-1 2014 Hemoglobin (Hb) as an important iron-containing oxygen-transport protein is easily oxidized to the ferric met-form, methemoglobin (metHb), and loses the capacity of binding oxygen during storage. Oxygen 48-54 hemoglobin subunit gamma 2 Homo sapiens 131-136 24342540-5 2014 This study provides insight into a new design for Hb-oxygen based carriers with strongly inhibition of metHb formation in aqueous environment under aerobic conditions, even at physiological temperature in vitro. Oxygen 53-59 hemoglobin subunit gamma 2 Homo sapiens 103-108 23469813-1 2014 Methemoglobin concentration is an important pathophysiological biomarker, reflecting the oxygen-carrying and oxygen-releasing capabilities of hemoglobin (Hb). Oxygen 89-95 hemoglobin subunit gamma 2 Homo sapiens 0-13 23469813-1 2014 Methemoglobin concentration is an important pathophysiological biomarker, reflecting the oxygen-carrying and oxygen-releasing capabilities of hemoglobin (Hb). Oxygen 109-115 hemoglobin subunit gamma 2 Homo sapiens 0-13 23201463-2 2013 MetHb is produced in the RBC by irreversible NO-induced oxidation of the oxygen carrying ferrous ion (Fe(2+)) present in the heme group of the hemoglobin (Hb) molecule to its non-oxygen binding ferric state (Fe(3+)). Oxygen 179-185 hemoglobin subunit gamma 2 Homo sapiens 0-5 24502349-0 2014 A new (G)gamma-globin variant causing low oxygen affinity: Hb F-Brugine/Feldkirch [(G)gamma105(G7)Leu His; HBG2: c.317T>A]. Oxygen 42-48 hemoglobin subunit gamma 2 Homo sapiens 107-111 21642830-1 2013 Methemoglobinemia occurs when hemoglobin is oxidized to form methemoglobin (MetHb) rendering it incapable of oxygen transport and leading to tissue hypoxia. Oxygen 109-115 hemoglobin subunit gamma 2 Homo sapiens 61-74 21642830-1 2013 Methemoglobinemia occurs when hemoglobin is oxidized to form methemoglobin (MetHb) rendering it incapable of oxygen transport and leading to tissue hypoxia. Oxygen 109-115 hemoglobin subunit gamma 2 Homo sapiens 76-81 24475977-5 2013 After oxygen therapy, the blood methemoglobin concentration level decreased to 2.1%, and the symptoms were alleviated. Oxygen 6-12 hemoglobin subunit gamma 2 Homo sapiens 32-45 23201463-1 2013 Methemoglobinemia is a disease that results from abnormally high levels of methemoglobin (MetHb) in the red blood cell (RBC), which is caused by simultaneous uptake of oxygen (O(2)) and nitric oxide (NO) in the human lungs. Oxygen 168-174 hemoglobin subunit gamma 2 Homo sapiens 75-88 23201463-1 2013 Methemoglobinemia is a disease that results from abnormally high levels of methemoglobin (MetHb) in the red blood cell (RBC), which is caused by simultaneous uptake of oxygen (O(2)) and nitric oxide (NO) in the human lungs. Oxygen 168-174 hemoglobin subunit gamma 2 Homo sapiens 90-95 23460588-2 2013 Here, we describe a novel fetal methemoglobin variant discovered in a newborn found to have oxygen saturations significantly below normal upon pulse oximetry screening for congenital heart disease. Oxygen 92-98 hemoglobin subunit gamma 2 Homo sapiens 32-45 20007731-1 2010 BACKGROUND: Methemoglobin in the blood cannot be detected by conventional pulse oximetry, although it can bias the oximeter"s estimate (Spo2) of the true arterial functional oxygen saturation (Sao2). Oxygen 174-180 hemoglobin subunit gamma 2 Homo sapiens 12-25 23662713-4 2013 Processes of metHb reduction and nitrosylation had the lag phase that was dependent on the presence of oxygen (O2) in the reaction mixture. Oxygen 103-109 hemoglobin subunit gamma 2 Homo sapiens 13-18 23662713-4 2013 Processes of metHb reduction and nitrosylation had the lag phase that was dependent on the presence of oxygen (O2) in the reaction mixture. Oxygen 111-113 hemoglobin subunit gamma 2 Homo sapiens 13-18 21964540-1 2011 Hydrogen peroxide triggers a redox cycle between methemoglobin and ferrylhemoglobin, leading to protein inactivation and oxygen evolution. Oxygen 121-127 hemoglobin subunit gamma 2 Homo sapiens 49-62 21964540-2 2011 In the present paper, the catalase-like oxygen production by human methemoglobin in the presence of H(2)O(2) was kinetically characterized with a Clark-type electrode. Oxygen 40-46 hemoglobin subunit gamma 2 Homo sapiens 67-80 22219589-3 2011 Methemoglobinemia is treated with supplemental oxygen and methylene blue (1-2 mg/kg) administered slow intravenously, which acts by providing an artificial electron acceptor for NADPH methemoglobin reductase. Oxygen 47-53 hemoglobin subunit gamma 2 Homo sapiens 184-197 23201463-1 2013 Methemoglobinemia is a disease that results from abnormally high levels of methemoglobin (MetHb) in the red blood cell (RBC), which is caused by simultaneous uptake of oxygen (O(2)) and nitric oxide (NO) in the human lungs. Oxygen 176-181 hemoglobin subunit gamma 2 Homo sapiens 75-88 23201463-1 2013 Methemoglobinemia is a disease that results from abnormally high levels of methemoglobin (MetHb) in the red blood cell (RBC), which is caused by simultaneous uptake of oxygen (O(2)) and nitric oxide (NO) in the human lungs. Oxygen 176-181 hemoglobin subunit gamma 2 Homo sapiens 90-95 23201463-2 2013 MetHb is produced in the RBC by irreversible NO-induced oxidation of the oxygen carrying ferrous ion (Fe(2+)) present in the heme group of the hemoglobin (Hb) molecule to its non-oxygen binding ferric state (Fe(3+)). Oxygen 73-79 hemoglobin subunit gamma 2 Homo sapiens 0-5 22885163-1 2012 During investigations of the phenotypic diversity of hemoglobin (Hb) E beta thalassemia, a patient was encountered with persistently high levels of methemoglobin associated with a left-shift in the oxygen dissociation curve, profound ascorbate deficiency, and clinical features of scurvy; these abnormalities were corrected by treatment with vitamin C. Oxygen 198-204 hemoglobin subunit gamma 2 Homo sapiens 148-161 20723561-5 2010 Results show that antioxidant enzymes helped minimize methemoglobin (non-carrier of oxygen) formation during the conjugation process and also during storage at 4 C over a period of 1 month. Oxygen 84-90 hemoglobin subunit gamma 2 Homo sapiens 54-67 20841412-1 2010 BACKGROUND: Methemoglobin in the blood cannot be detected by conventional pulse oximetry and may bias the oximeter"s estimate (Spo(2)) of the true arterial functional oxygen saturation (Sao(2)). Oxygen 167-173 hemoglobin subunit gamma 2 Homo sapiens 12-25 20841412-12 2010 CONCLUSIONS: The Rainbow"s methemoglobin readings are acceptably accurate over an oxygen saturation range of 74%-100% and a methemoglobin range of 0%-14%. Oxygen 82-88 hemoglobin subunit gamma 2 Homo sapiens 27-40 19617227-3 2009 As metHb cannot carry oxygen, clinical sequelae result when the concentration of metHb is high enough to compromise oxygen delivery to the tissues. Oxygen 22-28 hemoglobin subunit gamma 2 Homo sapiens 81-86 20306428-1 2010 Methemoglobinemia; an increased concentration of methemoglobin in the blood, is an altered state of hemoglobin whereby the ferrous form of iron is oxidized to the ferric state, rendering the heme moiety incapable of carrying oxygen. Oxygen 225-231 hemoglobin subunit gamma 2 Homo sapiens 49-62 21387795-3 2010 A molecule of methemoglobin is incapable of binding and carrying of oxygen. Oxygen 68-74 hemoglobin subunit gamma 2 Homo sapiens 14-27 21387795-7 2010 Cyanosis resistant to oxygen therapy and dyspnea occur in patients with the methemoglobin concentration above 20%. Oxygen 22-28 hemoglobin subunit gamma 2 Homo sapiens 76-89 19617227-3 2009 As metHb cannot carry oxygen, clinical sequelae result when the concentration of metHb is high enough to compromise oxygen delivery to the tissues. Oxygen 116-122 hemoglobin subunit gamma 2 Homo sapiens 3-8 19617227-3 2009 As metHb cannot carry oxygen, clinical sequelae result when the concentration of metHb is high enough to compromise oxygen delivery to the tissues. Oxygen 116-122 hemoglobin subunit gamma 2 Homo sapiens 81-86 18464252-8 2008 The results achieved are promising for the fabrication of blood substitutes with controlled metHb level, which can fulfill the binding/delivering oxygen to tissues in vivo for future trials. Oxygen 146-152 hemoglobin subunit gamma 2 Homo sapiens 92-97 19082413-1 2008 BACKGROUND AND OBJECTIVES: Methemoglobin is the oxidized form of hemoglobin, which does not bind oxygen and increases the affinity of oxygen for the partially oxidized portion of hemoglobin. Oxygen 134-140 hemoglobin subunit gamma 2 Homo sapiens 27-40 18478813-6 2008 Adequate oxygen delivery to the tissues in the body is compromised when MHb overwhelms the capacity of the red blood cells to carry oxygen. Oxygen 9-15 hemoglobin subunit gamma 2 Homo sapiens 72-75 18584368-6 2008 RESULTS: The remainder spectrum appears to be a methemoglobin variant quantitatively dependant on the amount of hydroxocobalamin added to the hemoglobin solution and the presence of oxygen. Oxygen 182-188 hemoglobin subunit gamma 2 Homo sapiens 48-61 18478813-6 2008 Adequate oxygen delivery to the tissues in the body is compromised when MHb overwhelms the capacity of the red blood cells to carry oxygen. Oxygen 132-138 hemoglobin subunit gamma 2 Homo sapiens 72-75 17982448-4 2007 The oxygen-bound form of nitrite-methemoglobin shows a degree of ferrous nitrogen dioxide (Fe(II)-NO2*) character, so it may rapidly react with NO to form N2O3. Oxygen 4-10 hemoglobin subunit gamma 2 Homo sapiens 33-46 18158911-5 2008 Nitric oxide has been reported to react easily with oxygen captured in hemoglobin to form nitrate, but not toxic free radicals, which may result in production of methemoglobin for the cytochrome b5 to regenerate functional ferrous hemoglobin. Oxygen 52-58 hemoglobin subunit gamma 2 Homo sapiens 162-175 18086531-4 2008 Accordingly, the O2-binding ability of the protein increases by short-time UVA irradiation of metHb together with NADH, which corresponds with the reduction of metHb, while it decreases by long-time UVA irradiation, which corresponds with the structural destruction. Oxygen 17-19 hemoglobin subunit gamma 2 Homo sapiens 94-99 18086531-4 2008 Accordingly, the O2-binding ability of the protein increases by short-time UVA irradiation of metHb together with NADH, which corresponds with the reduction of metHb, while it decreases by long-time UVA irradiation, which corresponds with the structural destruction. Oxygen 17-19 hemoglobin subunit gamma 2 Homo sapiens 160-165 14632342-8 2003 She received oxygen for 8 h until the methemoglobin level dropped to 1%. Oxygen 13-19 hemoglobin subunit gamma 2 Homo sapiens 38-51 17615278-1 2007 The reaction of nitrite with deoxyhemoglobin results in the production of nitric oxide and methemoglobin, a reaction recently proposed as an important oxygen-sensitive source of vasoactive nitric oxide during hypoxic and anoxic stress, with several animal studies suggesting that nitrite may have therapeutic potential. Oxygen 151-157 hemoglobin subunit gamma 2 Homo sapiens 91-104 16986127-2 2007 Hemoglobin has iron in the reduced valance Fe(II) and methemoglobin has iron in the oxidized valance Fe (III), with a free energy capable of producing water from oxygen. Oxygen 162-168 hemoglobin subunit gamma 2 Homo sapiens 54-67 18605250-3 2007 Methemoglobinemia is an abnormal elevation of MHb levels resulting in impaired oxygen delivery to tissues as well as a left shift of the oxygen-Hb dissociation curve. Oxygen 79-85 hemoglobin subunit gamma 2 Homo sapiens 46-49 15366957-0 2004 Reduction of methemoglobin via electron transfer from photoreduced flavin: restoration of O2-binding of concentrated hemoglobin solution coencapsulated in phospholipid vesicles. Oxygen 90-92 hemoglobin subunit gamma 2 Homo sapiens 13-26 17090432-1 2006 Hemoglobin based oxygen carriers (HBOC) are resuspended in "excipients" consisting of Ringer"s D,L-lactate containing antioxidants to prevent methemoglobin formation during storage. Oxygen 17-23 hemoglobin subunit gamma 2 Homo sapiens 142-155 11969358-2 2002 However, it also oxidizes hemoglobin to methemoglobin (metHgb), thereby reducing the delivery of oxygen to tissues. Oxygen 97-103 hemoglobin subunit gamma 2 Homo sapiens 40-53 12756430-1 2003 Methemoglobinemia, an increased concentration of methemoglobin in the blood, is an altered state of hemoglobin whereby the ferrous form of iron is oxidized to the ferric state, rendering the heme moiety incapable of carrying oxygen. Oxygen 225-231 hemoglobin subunit gamma 2 Homo sapiens 49-62 12911193-2 2003 Methemoglobin is incapable of carrying O2, and high levels may impact on O2 delivery to the tissues. Oxygen 39-41 hemoglobin subunit gamma 2 Homo sapiens 0-13 12911193-2 2003 Methemoglobin is incapable of carrying O2, and high levels may impact on O2 delivery to the tissues. Oxygen 73-75 hemoglobin subunit gamma 2 Homo sapiens 0-13 12854870-19 2003 Methemoglobin-forming agents are potent, but due to the transformation of hemoglobin into methemoglobin, they impair tissue delivery of oxygen. Oxygen 136-142 hemoglobin subunit gamma 2 Homo sapiens 0-13 12854870-19 2003 Methemoglobin-forming agents are potent, but due to the transformation of hemoglobin into methemoglobin, they impair tissue delivery of oxygen. Oxygen 136-142 hemoglobin subunit gamma 2 Homo sapiens 90-103 12754789-5 2003 The presence of different NO-hemoglobin derivatives can differently influence on the whole blood hemoglobin-oxygen affinity (HOA): methemoglobin and SNO-Hb increases, and HbFe2+NO decreases it. Oxygen 108-114 hemoglobin subunit gamma 2 Homo sapiens 131-144 12130498-4 2002 In support, hemoglobin in plasma, when oxidized to methemoglobin by oxidants such as leukocyte-derived reactive oxygen, causes oxidative modification of LDL. Oxygen 112-118 hemoglobin subunit gamma 2 Homo sapiens 51-64 10050328-1 1998 Oxygen regimen of the organism was experimentally studied at the stages of oxygen entry, transport, and consumption in severe exotoxigenic shock caused by poisoning with methemoglobin-forming toxin during correction of this state by different intensive care methods. Oxygen 0-6 hemoglobin subunit gamma 2 Homo sapiens 170-183 10973828-2 2000 However, we had found that the NO donor compounds 2-(N, N-diethylamino)-diazenolate-2-oxide (DEANO) and S-nitrosocysteine (CysNO) caused increased oxygen affinity of red cells from both AA and SS individuals and also caused significant methemoglobin (metHb) formation. Oxygen 147-153 hemoglobin subunit gamma 2 Homo sapiens 236-249 10973828-2 2000 However, we had found that the NO donor compounds 2-(N, N-diethylamino)-diazenolate-2-oxide (DEANO) and S-nitrosocysteine (CysNO) caused increased oxygen affinity of red cells from both AA and SS individuals and also caused significant methemoglobin (metHb) formation. Oxygen 147-153 hemoglobin subunit gamma 2 Homo sapiens 251-256 9769507-7 1998 In blood, oxidation state of hemoglobin results from very complex phenomena and if the body struggles against methemoglobin formation to maintain oxygen transport, the oxidation of hemoglobin is sometimes useful to protect tissues against various and numerous endogenous radical or non-radical oxidizing agents. Oxygen 146-152 hemoglobin subunit gamma 2 Homo sapiens 110-123 9588101-21 1998 In the case of high level of MetHb the drug of choice is administration of hyperbaric oxygen, methylene blue, ascorbic acid intravenously or riboflavin in high doses. Oxygen 86-92 hemoglobin subunit gamma 2 Homo sapiens 29-34 9242936-1 1997 To assess the oxygen transport capacity and safety of Neo Red Cells (NRC) with the enzymatic reduction system of methemoglobin in vitro and in experimental animals. Oxygen 14-20 hemoglobin subunit gamma 2 Homo sapiens 113-126 8363114-8 1993 The total oxygen-carrying capacity reduced by the combination of carboxyhemoglobin and methemoglobin was never more than 21% (range, 10% to 21%) in this series. Oxygen 10-16 hemoglobin subunit gamma 2 Homo sapiens 87-100 8048968-3 1994 The aim of the present study was to investigate the relationship between methemoglobin (metHb)-induced lipid peroxidation, rose bengal luminescence, and O2 consumption in a system containing 0-850 mu M phospholipid and 1 mu M metHb and 1 mu M rose bengal in Tris-HCl buffer, pH 7.4. Oxygen 153-155 hemoglobin subunit gamma 2 Homo sapiens 73-86 8148419-3 1994 The purified abnormal hemoglobin, like Hb J Cape Town, another variant of position alpha 92(FG4), displayed only a 1.5- to 2-fold increased oxygen affinity and a reduced cooperativity. Oxygen 140-146 hemoglobin subunit gamma 2 Homo sapiens 13-32 8241293-2 1993 This abnormal hemoglobin displays a very high oxygen affinity and a markedly reduced cooperativity that is partly restored in the presence of IHP. Oxygen 46-52 hemoglobin subunit gamma 2 Homo sapiens 5-24 9312831-13 1997 The purpose of these modifications is to modulate the affinity for O2 (by decreasing the binding of O2 and increasing its delivery to tissue), to reduce the dissociation into monomers and to guard against oxidation into methemoglobin. Oxygen 67-69 hemoglobin subunit gamma 2 Homo sapiens 220-233 8913407-7 1996 Oxidized hemoglobin, methemoglobin, is incapable of reversibly binding oxygen at the physiologic partial oxygen pressure. Oxygen 71-77 hemoglobin subunit gamma 2 Homo sapiens 21-34 8913407-7 1996 Oxidized hemoglobin, methemoglobin, is incapable of reversibly binding oxygen at the physiologic partial oxygen pressure. Oxygen 105-111 hemoglobin subunit gamma 2 Homo sapiens 21-34 8711189-10 1996 However, the elevated levels of methemoglobin and lactates indicate a slight degree of oxygen deficiency in the body. Oxygen 87-93 hemoglobin subunit gamma 2 Homo sapiens 32-45 1755337-1 1991 Some mechanisms to reduce methemoglobin (metHb) formation for the maintenance of normal oxygen transport have been proposed. Oxygen 88-94 hemoglobin subunit gamma 2 Homo sapiens 26-39 8353957-1 1993 When cyanide poisoning is treated with a methemoglobin-forming agent, oxidative metabolism is protected at the expense of the oxygen capacity of the blood. Oxygen 126-132 hemoglobin subunit gamma 2 Homo sapiens 41-54 8353957-2 1993 The affinity of methemoglobin for CN- is high enough to compete with cytochrome oxidase, which protects the latter from becoming blocked, but all hemoglobin used for this purpose is lost for the transport of oxygen. Oxygen 208-214 hemoglobin subunit gamma 2 Homo sapiens 16-29 8416301-1 1993 The ferrous iron of hemoglobin is exposed continuously to high concentrations of oxygen and, thereby, is oxidized slowly to methemoglobin, a protein unable to carry oxygen. Oxygen 81-87 hemoglobin subunit gamma 2 Homo sapiens 124-137 8117850-0 1993 Cross-linked hemoglobin-superoxide dismutase-catalase scavenges oxygen-derived free radicals and prevents methemoglobin formation and iron release. Oxygen 64-70 hemoglobin subunit gamma 2 Homo sapiens 106-119 1621630-4 1992 Nitrites are absorbed and form methemoglobin, which interferes with the oxygen-carrying capacity of hemoglobin. Oxygen 72-78 hemoglobin subunit gamma 2 Homo sapiens 31-44 1458186-2 1992 This action of OBQ was due to its capacity to activate the recovery of blood oxygen transport function by accelerating the restoration of methemoglobin and determined by their electron-acceptor properties, lipophilicity and NADP-dependent methemoglobin reductase affinity. Oxygen 77-83 hemoglobin subunit gamma 2 Homo sapiens 138-151 1716537-4 1991 The error in pulse oximetry caused by the presence of carboxyhemoglobin is insubstantial, but methemoglobin gives either an understimation or an overestimation at high or low oxygen saturation, respectively, the turning point being near 70% saturation. Oxygen 175-181 hemoglobin subunit gamma 2 Homo sapiens 94-107 2285779-3 1990 The fractional saturation with oxygen is evaluated by deconvoluting the optical absorption spectra, in the 500-700 nm wavelength region, in terms of oxyhemoglobin, deoxyhemoglobin and methemoglobin spectral components. Oxygen 31-37 hemoglobin subunit gamma 2 Homo sapiens 184-197 2285779-7 1990 Moreover, for equal amounts of methemoglobin the oxygen affinity is lower and the cooperativity higher for mixed samples than for those auto-oxidized. Oxygen 49-55 hemoglobin subunit gamma 2 Homo sapiens 31-44 35171971-0 2022 Scalable manufacturing platform for the production of methemoglobin as a non-oxygen carrying control material in studies of cell-free hemoglobin solutions. Oxygen 77-83 hemoglobin subunit gamma 2 Homo sapiens 54-67 35592205-1 2022 Methemoglobin (MetHb) is a form of hemoglobin in which iron in Hb is in an oxidized form (ferric) instead of ferrous, making it difficult to bind with oxygen. Oxygen 151-157 hemoglobin subunit gamma 2 Homo sapiens 0-13 35416740-19 2022 Oxygen therapy may well lead to complete recovery when methemoglobin levels do not exceed 30% in asymptomatic and 20% in mildly symptomatic patients. Oxygen 0-6 hemoglobin subunit gamma 2 Homo sapiens 55-68 34310360-4 2021 Sodium nitrite is used mostly in the food industry (as a preservative) and in medical field (as an antidote to cyanide poisoning), and if ingested in large enough amounts, it can be fatal.The ingestion of sodium nitrite can cause severe methemoglobinemia, which is a metabolic disorder characterized by an inability of hemoglobin (which gets oxidized into methemoglobin) to bind (and therefore carry) oxygen. Oxygen 401-407 hemoglobin subunit gamma 2 Homo sapiens 356-369 34760423-1 2021 Methemoglobinemia is caused due to an increase in methemoglobin in the blood, impairing oxygen transfer to tissues. Oxygen 88-94 hemoglobin subunit gamma 2 Homo sapiens 50-63 34703896-2 2021 Methemoglobin is incapable of binding oxygen, leading to complications such as cyanosis, dyspnea, headache, and heart failure. Oxygen 38-44 hemoglobin subunit gamma 2 Homo sapiens 0-13 35171971-1 2022 Methemoglobin (metHb) arises from the oxidation of ferrous hemoglobin (HbFe2+, Hb) to ferric hemoglobin (HbFe3+, metHb), which is unable to bind gaseous ligands such as oxygen (O2) and carbon monoxide (CO), and binds to nitric oxide (NO) significantly slower compared to Hb. Oxygen 169-175 hemoglobin subunit gamma 2 Homo sapiens 0-13 35171971-1 2022 Methemoglobin (metHb) arises from the oxidation of ferrous hemoglobin (HbFe2+, Hb) to ferric hemoglobin (HbFe3+, metHb), which is unable to bind gaseous ligands such as oxygen (O2) and carbon monoxide (CO), and binds to nitric oxide (NO) significantly slower compared to Hb. Oxygen 177-179 hemoglobin subunit gamma 2 Homo sapiens 0-13