{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T13:37:58Z","timestamp":1791898678212,"version":"4.3.4"},"reference-count":61,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2006,7,11]],"date-time":"2006-07-11T00:00:00Z","timestamp":1152576000000},"content-version":"vor","delay-in-days":4939,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American J Hematol"],"published-print":{"date-parts":[[1993,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    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. To restore hemoglobin function, methemoglobin (ferrihemoglobin) must be reduced to hemoglobin (ferrohemoglobin). Under physiological conditions, methemoglobin reduction is accomplished mainly by red cell NADH\u2010cytochrome b\n                    <jats:sub>5<\/jats:sub>\n                    reductase (NADH\u2010methemoglobin reductase) so efficiently that there is insignificant amounts of methemoglobin in the circulating blood. However, should methemoglobin formation be increased\u2014e.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\n                    <jats:sub>5<\/jats:sub>\n                    reductase\u2014methemoglobinemia will result. Most methemoglobinemias have no adverse clinical consequences and need not be treated. Under certain conditions, such as exposure to large amounts of oxidant or in young infants, rapid treatment is necessary. In hereditary cytochrome b\n                    <jats:sub>5<\/jats:sub>\n                    deficiency, treatment is often directed at improving the poor cosmetic effect of persistent cyanosis with the minimum amount of drugs to give satisfactory clinical results. \u00a9 1993 Wiley\u2010Liss, Inc.\n                  <\/jats:p>","DOI":"10.1002\/ajh.2830420104","type":"journal-article","created":{"date-parts":[[2007,2,21]],"date-time":"2007-02-21T07:51:28Z","timestamp":1172044288000},"page":"7-12","source":"Crossref","is-referenced-by-count":278,"title":["Methemoglobinemia"],"prefix":"10.1002","volume":"42","author":[{"given":"Ali","family":"Mansouri","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aubrey A.","family":"Lurie","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2006,7,11]]},"reference":[{"key":"e_1_2_1_2_2","first-page":"2267","volume-title":"The Metabolic Basis of Inherited Disease","author":"Jaff\u00e9 ER","year":"1989"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF01966121"},{"key":"e_1_2_1_4_2","first-page":"85","article-title":"Autoxische Zyanose (Intraglobulare Meth\u00e4moglobinemie)","volume":"23","author":"Hitzenberger K","year":"1932","journal-title":"Wien Arch Inn Med"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj0370615"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj0420013"},{"key":"e_1_2_1_7_2","first-page":"145","article-title":"Familial idiopathic methaemoglobinaemia and its treatment with ascorbic acid","volume":"5","author":"Barcroft H","year":"1945","journal-title":"Clin Sci"},{"key":"e_1_2_1_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-3002(59)90324-5"},{"key":"e_1_2_1_9_2","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/S0021-9258(18)81394-1","article-title":"Purification and properties of diphosphopyridine nucleotide diaphorase of human erythrocytes","volume":"237","author":"Scott EM","year":"1962","journal-title":"J Biol Chem"},{"key":"e_1_2_1_10_2","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/S0021-9258(18)97676-3","article-title":"The reduced pyridine nucleotide dehydrogenases of human erythrocytes","volume":"240","author":"Scott EM","year":"1965","journal-title":"J Biol Chem"},{"key":"e_1_2_1_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2744(67)90075-7"},{"key":"e_1_2_1_12_2","doi-asserted-by":"publisher","DOI":"10.1038\/1841651a0"},{"key":"e_1_2_1_13_2","doi-asserted-by":"publisher","DOI":"10.1038\/newbio229252a0"},{"key":"e_1_2_1_14_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.84.11.3609"},{"key":"e_1_2_1_15_2","doi-asserted-by":"crossref","first-page":"1408","DOI":"10.1182\/blood.V75.7.1408.1408","article-title":"Serine\u2010Proline replacement at residue 127 of NADH\u2010Cytochrome b5 reductase causes hereditary methemoglobinemia, Generalized Type","volume":"75","author":"Kobayashi Y","year":"1990","journal-title":"Blood"},{"key":"e_1_2_1_16_2","first-page":"799","article-title":"Exonic point mutations in NADH\u2010cytochrome b5 reductase genes of homozygotes for hereditary methemoglobinemias, types I and III: Putative mechanisms of tissue\u2010dependent enzyme deficiency","volume":"48","author":"Katsube T","year":"1991","journal-title":"Am J Hum Genet"},{"key":"e_1_2_1_17_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI102067"},{"key":"e_1_2_1_18_2","doi-asserted-by":"publisher","DOI":"10.1038\/202607a0"},{"key":"e_1_2_1_19_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00748a020"},{"key":"e_1_2_1_20_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00713a021"},{"key":"e_1_2_1_21_2","doi-asserted-by":"publisher","DOI":"10.1038\/202083b0"},{"key":"e_1_2_1_22_2","doi-asserted-by":"crossref","first-page":"1871","DOI":"10.1016\/S0021-9258(18)93522-2","article-title":"The electronic structure of protoheme proteins III. Configuration of the heme and its ligands","volume":"243","author":"Peisach J","year":"1968","journal-title":"J Biol Chem"},{"key":"e_1_2_1_23_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.67.4.1846"},{"key":"e_1_2_1_24_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)44679-6"},{"key":"e_1_2_1_25_2","first-page":"634","volume-title":"Hemoglobin: Molecular, genetic and clinical aspects","author":"Bunn HF","year":"1986"},{"key":"e_1_2_1_26_2","doi-asserted-by":"publisher","DOI":"10.1097\/00003246-199107000-00030"},{"key":"e_1_2_1_27_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.77.4.1917"},{"key":"e_1_2_1_28_2","first-page":"397","article-title":"The enzymatic reduction of ferrihemoglobin II. Purification of a ferrihemoglobin reductase from human erythrocytes","volume":"146","author":"Hegesh E","year":"1967","journal-title":"Biochem Biophys Acta"},{"key":"e_1_2_1_29_2","doi-asserted-by":"crossref","first-page":"6072","DOI":"10.1016\/S0021-9258(18)61834-4","article-title":"Purification of reduced pyridine nucleotide dehydrogenase from human erythrocytes and methemoglobin reduction by the enzyme","volume":"246","author":"Sugita Y","year":"1971","journal-title":"J Biol Chem"},{"key":"e_1_2_1_30_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2728(72)90024-2"},{"key":"e_1_2_1_31_2","doi-asserted-by":"crossref","first-page":"2454","DOI":"10.1016\/S0021-9258(19)85913-6","article-title":"Characterization of the purified NADH\u2010cytochrome b5 reductase of human erythrocytes as a FAD\u2010containing enzyme","volume":"255","author":"Yubisui T","year":"1980","journal-title":"J Biol Chem"},{"key":"e_1_2_1_32_2","first-page":"556","article-title":"Studies on methemoglobin reductase II. The purification and molecular properties of reduced nicotinamide adenine dinucleotide\u2010dependent methemoglobin reductase","volume":"247","author":"Kuma F","year":"1972","journal-title":"J Biol Chem"},{"key":"e_1_2_1_33_2","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.jbchem.a135495"},{"key":"e_1_2_1_34_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF01946415"},{"key":"e_1_2_1_35_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(77)91683-7"},{"key":"e_1_2_1_36_2","first-page":"467","article-title":"Reduction of methemoglobin","volume":"22","author":"Scott EM","year":"1963","journal-title":"Fed Proc"},{"key":"e_1_2_1_37_2","first-page":"760","article-title":"TPNH\u2010methemoglobin reductase deficiency: A new red\u2010cell enzyme defect","volume":"70","author":"Sass MD","year":"1967","journal-title":"J Lab Clin Med"},{"key":"e_1_2_1_38_2","first-page":"417","article-title":"DPNH\u2010methemoglobin reductase deficiency and hereditary methemoglobinemia","volume":"8","author":"Jaff\u00e9 ER","year":"1971","journal-title":"Seminars in Hematol"},{"key":"e_1_2_1_39_2","doi-asserted-by":"publisher","DOI":"10.1016\/0002-9343(66)90037-4"},{"key":"e_1_2_1_40_2","first-page":"323","article-title":"Methemoglobin reduction\u2014Studies of the interaction between cell populations and and of the role of methylene blue","volume":"22","author":"Beutler E","year":"1963","journal-title":"Blood"},{"key":"e_1_2_1_41_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)73873-8"},{"key":"e_1_2_1_42_2","first-page":"49","volume-title":"Measurement of Hemoglobin Derivatives","author":"Dubowski KM","year":"1964"},{"key":"e_1_2_1_43_2","doi-asserted-by":"publisher","DOI":"10.1093\/clinchem\/25.8.1388"},{"key":"e_1_2_1_44_2","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1093\/clinchem\/23.7.1215","article-title":"Simultaneous determination of hemoglobin derivatives, oxygen content, oxygen capacity, and oxygen saturation in 10 microliters of whole blood","volume":"23","author":"Rossi\u2010Bernardi L","year":"1977","journal-title":"Clin Chem"},{"key":"e_1_2_1_45_2","doi-asserted-by":"crossref","first-page":"1304","DOI":"10.1093\/clinchem\/26.9.1304","article-title":"Measuring percent oxygen saturation of hemoglobin, percent carboxyhemoglobin and methemoglobin, hemoglobin, and concentrations of total hemoglobin and oxygen in blood of man, dog and baboon","volume":"26","author":"Dennis RC","year":"1980","journal-title":"Clin Chem"},{"key":"e_1_2_1_46_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM194809232391305"},{"key":"e_1_2_1_47_2","first-page":"81","article-title":"Enzymopenic hereditary methemoglobinemia. A clinical\/biochemical classification","volume":"12","author":"Jaff\u00e9 ER","year":"1986","journal-title":"Blood cells"},{"key":"e_1_2_1_48_2","first-page":"81","article-title":"La reduction enzymatique de la methemoglobin","volume":"34","author":"Kaplan JC","year":"1980","journal-title":"Expos Annu Biochim Med"},{"key":"e_1_2_1_49_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(87)91122-3"},{"key":"e_1_2_1_50_2","doi-asserted-by":"crossref","first-page":"1288","DOI":"10.1182\/blood.V66.6.1288.1288","article-title":"Hereditary methemoglobinemia due to cytochrome b5 reductase deficiency in blood cells without associated neurologic and mental disorders","volume":"66","author":"Tanishima K","year":"1985","journal-title":"Blood"},{"key":"e_1_2_1_51_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM198603203141206"},{"key":"e_1_2_1_52_2","first-page":"253","article-title":"Drug\u2010induced methemoglobinemia","volume":"10","author":"Smith RP","year":"1973","journal-title":"Semin Hematol"},{"key":"e_1_2_1_53_2","first-page":"3","volume-title":"Eleven Blue Men. The Medical Detectives","author":"Rouech\u00e9 B","year":"1981"},{"key":"e_1_2_1_54_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM199207093270221"},{"key":"e_1_2_1_55_2","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1093\/clinchem\/38.4.596","article-title":"Benzocaine adultered street cocaine in association with methemoglobinemia","volume":"38","author":"McKinney CD","year":"1992","journal-title":"Clin Chem"},{"key":"e_1_2_1_56_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.47.11.1758"},{"key":"e_1_2_1_57_2","doi-asserted-by":"publisher","DOI":"10.1038\/newbio237263a0"},{"key":"e_1_2_1_58_2","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1038\/newbio237259a0","article-title":"Structure and subunit interaction of haemoglobin M Milwaukee","volume":"237","author":"Perutz MF","year":"1972","journal-title":"Nat New Biol"},{"key":"e_1_2_1_59_2","doi-asserted-by":"publisher","DOI":"10.3109\/03630268008996225"},{"key":"e_1_2_1_60_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(72)90565-7"},{"key":"e_1_2_1_61_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-3476(61)80064-4"},{"key":"e_1_2_1_62_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0140-6736(78)92357-7"}],"container-title":["American Journal of Hematology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fajh.2830420104","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/ajh.2830420104","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,25]],"date-time":"2023-10-25T03:18:00Z","timestamp":1698203880000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/ajh.2830420104"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1993,1]]},"references-count":61,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1993,1]]}},"alternative-id":["10.1002\/ajh.2830420104"],"URL":"https:\/\/doi.org\/10.1002\/ajh.2830420104","archive":["Portico"],"relation":{},"ISSN":["0361-8609","1096-8652"],"issn-type":[{"value":"0361-8609","type":"print"},{"value":"1096-8652","type":"electronic"}],"subject":[],"published":{"date-parts":[[1993,1]]}}}