Methemoglobin reductase

Methemoglobin - an overview ScienceDirect Topic

Methemoglobin constitutes 3% or less of the total hemoglobin in normal humans. Under normal circumstances, these levels in humans are maintained at 1% or less by the methemoglobin reductase enzyme system (the reduced form of nicotinamide adenine dinucleotide [NADH]-dehydratase, [NADH]-diaphorase, erythrocyte cytochrome b 5) Red blood cells (RBCs) possess methemoglobin reductase activity that counters the ongoing oxidation of hemoglobin (Hb) to methemoglobin (metHb), which in circulating blood is caused by Hb autoxidation or reactions with nitrite Methemoglobin reductase deficiency is a rare condition in small animals that leads to inefficient reduction of methemoglobin in the body but may or may not lead to clinical signs of methemoglobinemia Spontaneously formed methemoglobin is normally reduced (regenerating normal hemoglobin) by protective enzyme systems, e.g., NADH methemoglobin reductase (cytochrome-b5 reductase) (major pathway), NADPH methemoglobin reductase (minor pathway) and to a lesser extent the ascorbic acid and glutathione enzyme systems. Disruptions with these enzyme systems lead to methemoglobinemia

Congenital methemoglobinemia is a relatively rare clinical disorder characterized by life-long cyanosis, caused by either an inherited mutant hemoglobin (Hb-M) or deficiency of physiologically active NADH-dependent methemoglobin reductase (NADH-MR). NADH-MR deficiency leads to two different types of recessive congenital methemoglobinemia The NADH-dependent enzyme methemoglobin reductase (a type of diaphorase) is responsible for converting methemoglobin back to hemoglobin. Normally one to two percent of a person's hemoglobin is methemoglobin; a higher percentage than this can be genetic or caused by exposure to various chemicals and depending on the level can cause health problems known as methemoglobinemia

Methemoglobin reductase activity in intact fish red blood

  1. In normal physiological conditions, methemoglobin is converted to hemoglobin by enzyme cytochrome b5 reductase (also known as methemoglobin reductase or b5R). Congenital methemoglobinemia, an autosomal recessive disorder, is most commonly due to a cytochrome b5 reductase (b5R) deficiency
  2. The NADH-methemoglobin reductase activity as well as hemoglobin and methemoglobin levels were investigated in blood samples of 182 adult leprosy patients and 137 Brazilian army enlisted men. The level of sulfones in the blood samples of the leprosy patients, all of them ingesting a daily dose of 100 mg dapsone, was also investigated
  3. There are two types of inherited MetHb: Type 1 (also called erythrocyte reductase deficiency) occurs when RBCs lack the enzyme. Type 2 (also called generalized reductase deficiency) occurs when the enzyme doesn't work in the body. The second form of inherited MetHb is called hemoglobin M disease
  4. Methemoglobinemia due to NADH-cytochrome b5 reductase deficiency is an autosomal recessive disorder characterized clinically by decreased oxygen carrying capacity of the blood, with resultant cyanosis and hypoxia (review by Percy and Lappin, 2008 ). There are 2 types of methemoglobin reductase deficiency
  5. The methemoglobin ferrocyanide reductase activity of the enzyme in erythrocyte hemolysates was 3.2-6.4% of normal. Electrophoresis of hemolysates prepared from the blood of patients from two different families at six pH values between 4.6 and 9.3 did not differentiate between the variant enzymes
  6. However, an abnormal value in an asymptomatic patient may suggest the presence of an elevated methemoglobin fraction. Treatment. Methylene blue is the first line. It accelerates the enzymatic reduction of methemoglobin by NADPH-methemoglobin reductase and also reduces to leucomethylene blue that, in turn, reduces methemoglobin

Abnormally increased levels of methemoglobin in the blood. In this form of hemoglobin, there is an oxidized ferric iron (Fe +3) rather than the reduced ferrous form (Fe 2+) that is normally found in hemoglobin. Methemoglobin has a reduced affinity for oxygen, resulting in a reduced ability to release oxygen to tissues By far the most significant means of effecting this electron gain is an enzyme-reducing system present in red cells, known as NADH-dependent cytochrome b5-methemoglobin reductase. Under physiological conditions this system accounts for close to 99 % of the daily methemoglobin reduction to hemoglobin

  1. A small but constant amount of methemoglobin is produced in the red blood cells. It is reduced by specific enzymes (methemoglobin reductases) and NADH, which is generated in glycolysis. Reductases isolated from human red cells also use NADPH, but to a lesser extent. Inability to reduce metHb produces methemoglobinemia and tissue anoxia
  2. Methemoglobinemia is a blood disorder that occurs when too little oxygen is delivered to the cells of the body. There are two kinds of methemoglobinemia — congenital and acquired
  3. Methemoglobin reduction by NADH-cytochrome b(5) reductase in Propsilocerus akamusi larvae Comp Biochem Physiol B Biochem Mol Biol . 2015 Jul;185:54-61. doi: 10.1016/j.cbpb.2015.03.006
  4. An alternate pathway for the reduction of methemoglobin is through the function of nicotinamide adenine dinucleotide phosphate hydrogen methemoglobin (NADPH-MetHb) reductase. NADPH-MetHb reductase utilizes NADPH that forms through the action of glucose-6-phosphate dehydrogenase (G6PD) in the hexose monophosphate shunt, for its reducing power. Under normal physiologic circumstances, NADPH-MetHb reductase contributes very little to the reduction of methemoglobin, but under oxidative stress.
  5. NADH + H + + 2 ferricytochrome b5 = NAD + + 2 ferrocytochrome b5 In its b5-reducing capacity, this enzyme is involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, and drug metabolism. This enzyme can also reduce methemoglobin to normal hemoglobin, gaining it the inaccurate synonym methemoglobin reductase
  6. The membrane methemoglobin reductase-like activity is unmasked by Triton X-100 treatment, and represents about half of the total activity in the erythrocytes. Like the amphiphilic microsomal-bound cytochrome b5 reductase, the erythrocyte membrane-bound enzyme is solubilized by cathepsin D
  7. Methemoglobinemia is a condition characterized by elevated levels of methemoglobin in the blood. Methemoglobin is the oxidized form of hemoglobin, where the heme iron has been converted from the usual ferrous (Fe 2+) to the ferric (Fe 3+) form.The Fe 3+ form of iron cannot bind O 2, and, thus, leads to tissue hypoxia.Methemoglobinemia results from congenital defects or can occur after exposure.

Methemoglobinemia - Wikipedi

  1. ant mode
  2. The organic phosphate allosteric effectors of hemoglobin, inositol hexaphosphate, 2,3-diphosphoglycerate, and ATP, interact with NADH-methemoglobin reductase (NADH-diaphorase). Significant inhibitory effects on the enzyme were found when dichlorophenolindophenol, or ferricyanide were used as electron acceptors in place of methemoglobin
  3. Methemoglobin reductase maintains this balance. Therefore, a disruption in this system will cause an imbalanced level of oxidized hemoglobin. May be caused by: Prilocaine metabolites (most common - usually appearing after a dose of greater than or equal to 8 mg/kg
  4. However, should methemoglobin formation be increased—e.g., due to the presence of oxidant drugs, or an abnormal methemoglobin not amenable to reduction (hemoglobin M), or a deficiency in red cell cytochrome b 5 reductase—methemoglobinemia will result. Most methemoglobinemias have no adverse clinical consequences and need not be treated
  5. g cases of heterozygous or homozygous methemoglobin reductase deficiency; genetic studies in families with methemoglobin reductase deficiency. Reference Range * 6.6 - 13.3 U/g hemoglobin * Reference ranges may change over time. Please refer to the original patient report when evaluating results
  6. The primary mode of MetHb reduction, accounting for 99% of daily MetHb reduction, is the cytochrome [b.sub.5] methemoglobin reductase (NADH methemoglobin reductase) system (26). Infants are particularly susceptible to toxin-induced methemoglobinemia because of lowered erythrocyte cytochrome bs methemoglobin reductase activity (50-60% of adult.

In type I, which is the most common type, cytochrome b5 reductase is absent only in red blood cells, and methemoglobin levels typically range from 10-35%. Type II methemoglobinemia is much more severe because cytochrome b5 reductase is absent in every cell in the body, and methemoglobin levels are much higher than 35% Due to a deficiency of the enzyme diaphorase I (cytochrome b5 reductase), methemoglobin levels rise and the blood of met-Hb patients has reduced oxygen-carrying capacity. Instead of being red in color, the arterial blood of met-Hb patients is brown. This results in the skin of Caucasian patients gaining a bluish hue Methemoglobin, sulfhemoglobin levels, cytochrome-b5 reductase (methemoglobin reductase) activity, and protein analysis screening for hemoglobin (Hb) variants (capillary electrophoresis, cation exchange high performance liquid chromatography [HPLC] and capillary electrophoresis) will always be performed

Methemoglobin is unable to bind oxygen, and elevated level of methemoglobin or methemoglobinemia, can lead to cyanosis and be life-threatening. A small amount of Fe2+ oxidizes to Fe3+ everyday but at the same time, methemoglobin converts back to hemoglobin through reducing activity of cytochrome b5-reductase Methemoglobinemia is a blood disorder in which too little oxygen is delivered to your cells. Oxygen is carried through your bloodstream by hemoglobin, a protein that's attached to your red blood. Methemoglobin (British: methaemoglobin) (pronounced met-hemoglobin) is a hemoglobin in the form of metalloprotein, in which the iron in the heme group is in the Fe 3+ state, not the Fe 2+ of normal hemoglobin.Methemoglobin cannot bind oxygen, which means it cannot carry oxygen to tissues. It is bluish chocolate-brown in color. In human blood a trace amount of methemoglobin is normally. NADH MetHb reductase keeps oxidative stress in check by reducing MetHb to Fe 2+ state; Methemoglobinemia occurs when either. There is an deficiency of the reducing enzyme (NADH MetHb reductase) There is increased oxidative stress that cannot be handled by the body; Presence of MetHb renders pulse-oximetry readings inaccurate; Common Causative.

Congenital methemoglobinemia due to NADH-methemoglobin

  1. Animated Mnemonics (Picmonic): https://www.picmonic.com/viphookup/medicosis/ - With Picmonic, get your life back by studying less and remembering more. M..
  2. Related tests/panels: The methemoglobin level is tested as part of a series of tests in the evaluation of methemoglobinemia. Additional tests include hemoglobin A2 and F, hemoglobin electrophoresis, sulfhemoglobin, and methemoglobin reductase
  3. The cytochrome b 5 reductase deficiency seems to manifest methemoglobinemia through the decrease in the enzymatic reduction of cytochrome b 5 and subsequent nonenzymatic reduction of methemoglobin by the reduced cytochrome b 5. The methemoglobinemic diaphorase II was found similar to the normal enzyme with respect to Kms for the dye and NADH.
  4. Methemoglobin reductase which is responsible for the re- duction of methemoglobin in erythrocyetes has been purified to a homogeneous form by Kuma et al. (1, 2), who have demonstrated that the enzyme is a flavoprotein, having flavin adenine dinucleotide as a prosthetic group, and that its mo
  5. Inherited methemoglobinemia is a rare disorder caused by a deficiency of the enzyme methemoglobin reductase, by the synthesis of an abnormal enzyme, or by the presence of an abnormal hemoglobin (hemoglobin M). Although cyanotic from birth, patients who have inherited methemoglobinemia are otherwise well
  6. Methemoglobin Reductase, B. Test Resources. None found for this test Please visit our Clinical Education Center to stay informed on any future publications, webinars, or other education opportunities. Test Details. Methodology. Kinetic Spectrophotometric (KS) Reference Range(s

Cytochrome-b 5 reductase is a NADH-dependent enzyme that converts ferricytochrome from a Fe3+ form to a Fe2+ form.It contains FAD and catalyzes the reaction: . NADH + H + + 2 ferricytochrome b 5 = NAD + + 2 ferrocytochrome b 5. In its b5-reducing capacity, this enzyme is involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, and drug metabolism Useful ForSuggests clinical disorders or settings where the test may be helpful. Evaluation of patients with cyanosis. Confirming cases of suspected cytochrome b5 reductase (methemoglobin reductase) deficiency. Functional studies in families with cytochrome b5 reductase deficiency methemoglobin [met-he´mo-glo″bin] a hematogenous pigment formed from hemoglobin by oxidation of the iron atom from the ferrous to the ferric state. A small amount is found in the blood normally, but injury or toxic agents convert a larger proportion of hemoglobin into methemoglobin, which does not function as an oxygen carrier. Miller-Keane. The risk for adverse effects associated with prilocaine use is increased for infants, persons with underlying health problems (i.e., anemia or diseases affecting the respiratory or cardiovascular systems), persons with hereditary deficiencies of glucose-6-phosphate dehydrogenase and methemoglobin reductase, and persons taking other oxidant drugs (e.g., nitrite-containing medications.

Methemoglobinemia Hemoglobin M disease; Erythrocyte reductase deficiency; Generalized reductase deficiency; MetHb. Methemoglobinemia (MetHb) is a blood disorder in which an abnormal amount of methemoglobin is produced. Hemoglobin is the protein in red blood cells (RBCs) that carries and distributes oxygen to the body Methemoglobinemia may be due to a defect in the enzyme NADH methemoglobin reductase (an autosomal recessive trait) or to an abnormality in hemoglobin M (an autosomal dominant trait). (Dorland. methemoglobin reductase. Methemoglobin redüktaz; methemoglobin redüktaz. Oksijeni taşıyamayan methemoglobindeki Fe+3'ü NADPH veya NADH varlığında Fe+2'ye çeviren ve hemoglobini yeniden oksijen taşıyabilir duruma getiren enzim. Methemoglobin reductase

When hemoglobin contains ferric iron, it is methemoglobin. The soluble isoform of cytochrome b5 reductase 3 changes ferric iron back to ferrous iron so hemoglobin can deliver oxygen to tissues. Normally, red blood cells contain less than 2 percent methemoglobin. The membrane-bound isoform is widely used in the body Methemoglobin is produced as a result of normal oxidant stress and comprises approximately 3% of a person's total hemoglobin.2 Two primary adaptive mechanisms can re-strict this value to less than 1%: the cytochrome b5-MetHb reductase pathway and the NADPH-MetHb reductase pathway.2 The cytochrome b5-MetHb reductase pathway i Methemoglobin reductase pathway | Article about methemoglobin reductase pathway by The Free Dictionar Methemoglobinemia is a potentially life-threatening health condition in which the oxygen-carrying capacity of circulating hemoglobin is significantly reduced. Image Credit: MicroOne/Shutterstock.com Hereditary methemoglobinemia is rare. The most common cause of congenital methemoglobinemia is cytochrome b5 reductase deficiency (type Ib5R). This enzymatic deficiency is endemic in certain.

Methemoglobin - Wikipedi

  1. Definition of NADH-methemoglobin reductase in the Medical Dictionary by The Free Dictionar
  2. /mgprotein Unsealed ghosts-cathepsin D 57 0 0 Unsealedghosts +cathepsin D 21.3 12.3 36.6 Resealedghosts (inside-in) + cathepsin D 34 0 0 Ghosts prepared as described in text were incubated for 2
  3. Methemoglobinemia is characterized by an increase in the concentration of oxidized hemoglobin (iron in the ferric state). 1 Methemoglobin impairs the normal transport of oxygen to tissues, leading to cyanosis and exercise intolerance at concentrations >20%. 2, 3 The reduction in methemoglobin to hemoglobin primarily depends on nicotinamide adenine dinucleotide (NADH) methemoglobin reductase.
  4. NADH-methemoglobin reductase, was clearly shown to be absent in the erythrocyte of individuals with congenital met- hemoglobinemia. Since Scott first demonstrated the deficiency of NADH-diaphorase activity in congenital methemoglobinemia (2, 3), the true identity of this enzyme has been obscure since n
  5. ant trait). (Dorland, 27th ed) Concepts: Disease or Syndrome (T047) MS
  6. Congenital methemoglobinemia arises from globin mutations that stabilize iron in the ferric state (e.g., HbM Iwata [α87His→Tyr] or from mutations that impair the enzymes that reduce methemoglobin to hemoglobin (e.g., methemoglobin reductase, NADP diaphorase)
  7. - Heterozygotes at risk of developing acute, symptomatic methemoglobinemia after exposure to exogenous, methemoglobin-inducing agents MOLECULAR BASIS - Caused by mutation in the cytochrome b5 reductase 3 gene (CYB5R3, 613213.0001
Difference Between Reductase and Oxidoreductase | Compare

methemoglobin reductase enzymes were characterized imme-diately after purification. In vivo lability of NADHmethemoglobin reductase. 80-125-ml samples of blood were subjected to density separa-tion by differential flotation on mixtures of phthalate esters of known specific gravity (11). Portions of whole blood measuring 2.25 ml mixed with 0.75. Methemoglobin is an altered form of hemoglobin in which the ferrous state, Fe2+, loses an electron and is oxidized to the ferric, Fe3+, state. This change in the iron moiety renders hemoglobin incapable of carrying oxygen, leading to decreased oxygen delivery to tissues and a functional anemia. This process naturally occurs in the body at low. FLR had previously been isolated as an NADPH-dependent diaphorase, designated diaphorase-2 (DIA2), by Fisher et al. (1977) and has also been called methemoglobin reductase and NADPH reductase. Yubisui et al. (1977, 1979) found that flavins are the effective electron acceptor of the enzyme and purified FLR to homogeneity Define methemoglobin reductase pathway. methemoglobin reductase pathway synonyms, methemoglobin reductase pathway pronunciation, methemoglobin reductase pathway translation, English dictionary definition of methemoglobin reductase pathway. n. A brownish-red form of hemoglobin that occurs when hemoglobin is oxidized either during decomposition. of methemoglobin reductase or to a structural abnormality of hemoglobin, or it may be acquired, usually secondary to exposure to drugs or chemicals that oxidize hemoglobin, and occasionally are secondary to pathologic conditions, such as sepsis, sickle cell crisis, and gastrointestinal infections in children. Drugs have been implicate

מטהמוגלובינמיה, או כחלת (באנגלית: Methemoglobinemia) היא תסמונת המתרחשת כאשר תאי דם אדומים מכילים מטהמוגלובין ברמות גבוהות מ-1%. התסמונת מאופיינת בנוכחות גבוהה מהרגיל של מטהמוגלובין (metHb) בדם, כלומר של Fe +3 במקום Fe +2 NADH Methemoglobin Reductase Add NADH-Cytochrome B5 Reductase Add NADH-Ferrihemoglobin Reductase Add Pharm Action Registry Number EC Related Numbers 9032-25-1 EC CAS Type 1 Name NLM Classification # Previous Indexing Cytochrome Reductases (1975-2003). Special emphasis is directed to the major and minor metabolic pathways in human erythrocytes that are involved in the reduction of methemoglobin, and evidence is presented that the NADH-methemoglobin reductase system, involving a soluble cytochrome b5 and NADH-cytochrome b5 reductase, it is the most important reductive mechanism METHEMOGLOBIN REDUCTASE DEFICIENCY ORPHA: 621; Heme - No methemoglobinemia. Lab - NADPH-methemoglobin reductase deficiency - Abnormal red cell methylene-blue screening test - Normal red cell G6PD activity. Inheritance - Autosomal recessive [SNOMEDCT: 258211005]. Methemoglobin (tiếng Anh: methaemoglobin) (phát âm là met-hemoglobin) là một huyết sắc tố (hemoglobin) ở dạng metalloprotein, trong đó sắt trong nhóm heme ở trang thái Fe 3+, không phải ở trạng thái Fe 2+ của hemoglobin bình thường. Methemoglobin không thể liên kết với oxy, có nghĩa là không thể vận chuyển oxy đến các mô

Methemoglobinemia - an overview ScienceDirect Topic

NADH-methemoglobin reductase and methemoglobinemia among

Inherited methemoglobinemia can be of the following types: 1. Type 1: It is also known as erythrocyte reductase deficiency [10].It happens when RBCs lack the enzyme called cytochrome b5 reductase [11].. 2. Type 2: It is also known as generalized reductase deficiency [12].It happens when the enzyme called cytochrome b5 reductase does not work in the body Cytochrome B5 reductase (methemoglobin reductase) catalyzes the 1,4-dihydronicotinamide adenine dinucleotide (NADH)-linked reduction of several substrates, including ferricyanide. The activity at 30 degrees C is followed spectrophotometrically by measuring the oxidation of NADH at 340 nm.(Fairbank VF, Klee GG: Biochemical aspects of hematology The disorder recessive congenital methemoglobinemia (RCM; McKusick no. 250 800) is caused by a deficiency of reduced nicotinamide adenine dinucleotide (NADH)-cytochrome b5 reductase (cytb5r: E.C. Two forms of cytb5r are known, a soluble form and a membrane-bound form, and are localized in different cellular compartments MEVI : Interpretation of the methemoglobinemia evaluation results Diagnosis of methemoglobinemia and sulfhemoglobinemia and possible hereditary (congenital) causes Differentiation of methemoglobinemia and sulfhemoglobinemia from other causes of cyanosis (eg, congenital heart disease

Methemoglobinemia: MedlinePlus Medical Encyclopedi

Methemoglobinemia Due to Deficiency of Methemoglobin Reductas

Unstable variant of NADH methemoglobin reductase in Puerto

Methemoglobinemia: diagnosis - OpenAnesthesi

Methemoglobin reductase deficiency (Concept Id: C0472786

However, should methemoglobin formation be increased--e.g., due to the presence of oxidant drugs, or an abnormal methemoglobin not amenable to reduction (hemoglobin M), or a deficiency in red cell cytochrome b5 reductase--methemoglobinemia will result. Most methemoglobinemias have no adverse clinical consequences and need not be treated reduction in methemoglobin to hemoglobin primarily depends on nicotinamide adenine dinucleotide (NADH) methemoglobin reductase (NADH-cytochrome b5 reductase, b5R [EC.]).4 There are 2 forms of b5R: a membrane-bound form (the somatic form) and a soluble form (the erythrocytic form), which lacks the membrane anchor domain.5 Both types of.

Effects Of Industrial Emissions

Methemoglobin - acute care testin

NADPH methemoglobin reductase deficiency. blue from too much methylene blue (usually acute doses significantly > 7 mg/Kg). ingestion or exposure to a large dose of an etiologic agent or to a very strong oxidant with a long half-life. It is the latter situation (#6) I will address here The electrophoretic mobility and activity of NADH-methemoglobin reductase in erythrocytes of patients with hereditary methemoglobinemia, obligatory heterozygotes, and normal subjects were examined. Six distinct electrophoretic variants were found in studies of erythrocytes from members of ten different families

The blood blues: A review on methemoglobinemia David SRInterrelation of nitrate, nitrite, and the L-arginine

Cytochrome B5 Reductase - an overview ScienceDirect Topic

Methemoglobinemia: Monitor methemoglobin levels in patients with cardiopulmonary disease, hemoglobinopathy, or methemoglobin reductase deficiency Agranulocytosis: Monitor CBC count 4-10 wk after initiation of therapy; stop therapy when WBC count < 4000/[mm.sup.3] Peripheral neuropathy: Periodic neurologic screening examination by dermatologist; any suspected abnormality needs referral for full. A striking proportion of Algerian subjects was reported among patients with congenital recessive methemoglobinemia due to cytochrome b5 reductase deficiency (Kaplan et al. 1979). A population survery was carried out in red blood cells from 1000 algerian subjects. In 16 subjects, the cytochrome b5 reductase activity was diminished by 50%. Family studies indicated the presence of a defective. The membrane methemoglobin reductase-like activity is unmasked by Triton X-100 treatment, and represents about half of the total activity in the erythrocytes. Like the amphiphilic microsomal-bound cytochrome b5 reductase, the erythrocyte membrane-bound enzyme is solubilized by cathepsin D. Because this treatment is effective on unsealed ghosts.

Methemoglobinemia: Treatment, diagnosis, and type

Meta-hemoglobina é uma forma de proteína da hemoglobina, na qual o ferro no grupo hemo está no estado Fe 3+ e não no Fe 2+ da hemoglobina normal. A metemoglobina não pode ligar o oxigênio, ao contrário da oxi-hemoglobina.No sangue humano uma pequena quantidade de metemoglobina é normalmente produzida espontaneamente acid. NADPH-methemoglobin reductase plays a pivotal role in the treatment of methemoglobinemia. This enzyme will reduce dyes, such as methylene blue, which may then reduce methemoglobin to hemoglobin. Causes of Methemoglobinemia Exposure to an Oxidizing Agent The most common cause of methemoglobinemia is exposure to oxidant drugs or metabolites met·he·mo·glo·bin (mĕt-hē′mə-glō′bĭn) n. A brownish-red form of hemoglobin that occurs when hemoglobin is oxidized either during decomposition of the blood or by the action of various oxidizing drugs or toxic agents. It contains iron in the ferric state and cannot function as an oxygen carrier. [met(a)- + hemoglobin.] American Heritage.

Flavin reductase - WikipediaMethemoglobinemia – Core EMMethemoglobinemia
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