PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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. Ferric enterobactin ion 90-96 hemoglobin subunit gamma 2 Homo sapiens 0-13 17655520-1 2007 Methemoglobin, a form of hemoglobin that does not bind oxygen, is produced when iron in red blood cells is oxidized from the ferrous state to the ferric state. Ferric enterobactin ion 146-152 hemoglobin subunit gamma 2 Homo sapiens 0-13 30612358-5 2019 HgCl2 treatment resulted in oxidation of ferrous iron of hemoglobin to ferric form giving methemoglobin which is inactive as an oxygen transporter. Ferric enterobactin ion 71-77 hemoglobin subunit gamma 2 Homo sapiens 90-103 29185409-1 2017 Methemoglobin (MetHb) is a form of hemoglobin which contains iron in ferric state. Ferric enterobactin ion 69-75 hemoglobin subunit gamma 2 Homo sapiens 0-13 29185409-1 2017 Methemoglobin (MetHb) is a form of hemoglobin which contains iron in ferric state. Ferric enterobactin ion 69-75 hemoglobin subunit gamma 2 Homo sapiens 15-20 33256027-1 2020 Methemoglobin (MetHb) is a hemoglobin (Hb) derivative with the heme iron in ferric state (Fe3+), unable to deliver oxygen. Ferric enterobactin ion 76-82 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. Ferric enterobactin ion 76-82 hemoglobin subunit gamma 2 Homo sapiens 15-20 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+)). Ferric enterobactin ion 194-200 hemoglobin subunit gamma 2 Homo sapiens 0-5 11367578-2 2001 The photon intensity was affected by the ferric state of Hb (methemoglobin > oxyhemoglobin), and was roughly correlated with the radical-scavenging potential of catechins. Ferric enterobactin ion 41-47 hemoglobin subunit gamma 2 Homo sapiens 61-74