PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31727545-12 2019 DISCUSSION: Increase in non-haem iron prior to induction of HO-1 expression suggests the involvement of HO-2 in haem-induced cytotoxicity. Iron 33-37 heme oxygenase 2 Homo sapiens 104-108 33051205-1 2020 Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Iron 85-89 heme oxygenase 2 Homo sapiens 0-16 33051205-1 2020 Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Iron 85-89 heme oxygenase 2 Homo sapiens 18-21 31865128-3 2020 The inside mechanism of the LFUA process includes: 1) displacement of HMIs from HMI-EDTA complexes by Fe(III); 2) direct photolysis of Fe(III)-EDTA through a ligand-to-metal charge transition reaction (LMCT) and indirect photolysis of EDTA by HO2 /O2 -. Iron 102-109 heme oxygenase 2 Homo sapiens 243-246 31865128-5 2020 Fe(II) formed during the LMCT reaction of Fe(III)-EDTA was oxidized back to Fe(III) by O2 and HO2 , and the reformed Fe(III) was then recombined with EDTA to sustains the LMCT reaction. Iron 0-6 heme oxygenase 2 Homo sapiens 94-97 31865128-5 2020 Fe(II) formed during the LMCT reaction of Fe(III)-EDTA was oxidized back to Fe(III) by O2 and HO2 , and the reformed Fe(III) was then recombined with EDTA to sustains the LMCT reaction. Iron 42-49 heme oxygenase 2 Homo sapiens 94-97 31865128-5 2020 Fe(II) formed during the LMCT reaction of Fe(III)-EDTA was oxidized back to Fe(III) by O2 and HO2 , and the reformed Fe(III) was then recombined with EDTA to sustains the LMCT reaction. Iron 76-83 heme oxygenase 2 Homo sapiens 94-97 21647550-2 2012 On the other hand, oxidative stress has been implicated in the pathogenesis of age-related macular degeneration (AMD) and heme oxygenase-1 (HO-1), encoded by the HMOX1 gene and heme oxygenase-2 (HO-2), encoded by the HMOX2 gene are important markers of iron-related oxidative stress and its consequences. Iron 253-257 heme oxygenase 2 Homo sapiens 177-193 27892575-6 2016 The transition from the FeN4 structure to metallic Fe results in a significant loss in ORR activity and an increase in the production of undesirable HO2- during catalysis. Iron 24-26 heme oxygenase 2 Homo sapiens 149-152 27604527-1 2016 Heme oxygenases are composed of two isozymes, Hmox1 and Hmox2, that catalyze the degradation of heme to carbon monoxide (CO), ferrous iron, and biliverdin, the latter of which is subsequently converted to bilirubin. Iron 126-138 heme oxygenase 2 Homo sapiens 56-61 26652036-1 2016 The two isoforms of human heme oxygenase (HO1 and HO2) catalyze oxidative degradation of heme to biliverdin, Fe, and CO. Iron 109-111 heme oxygenase 2 Homo sapiens 50-53 24131232-1 2014 SIGNIFICANCE: Heme oxygenases (HO-1 and HO-2) catalyze the degradation of the pro-oxidant heme into carbon monoxide (CO), iron, and biliverdin, which is subsequently converted to bilirubin. Iron 122-126 heme oxygenase 2 Homo sapiens 40-44 24275768-1 2014 PURPOSE OF REVIEW: Heme oxygenase activity, possessed by an inducible heme oxygenase-1 (HO-1) and a constitutive isoform (HO-2), catalyzes the conversion of heme to biliverdin, liberates iron, and generates carbon monoxide. Iron 187-191 heme oxygenase 2 Homo sapiens 122-126 19473966-4 2009 Unlike HO-1, which lacks cysteine residues, HO-2 contains three Cys-Pro signatures, known as heme regulatory motifs (HRMs), which are known to control processes related to iron and oxidative metabolism in organisms from bacteria to humans. Iron 172-176 heme oxygenase 2 Homo sapiens 44-48 20502928-7 2010 Additionally, absorption, magnetic circular dichroism, and resonance Raman data collected at different temperatures reveal an intriguing temperature dependence of the iron spin state in the heme-HO-2 complex. Iron 167-171 heme oxygenase 2 Homo sapiens 195-199 21709601-2 2011 Heme oxygenase 2 (HMOX2) catalyzes the cleavage of the heme ring to form biliverdin with release of iron and carbon monoxide. Iron 100-104 heme oxygenase 2 Homo sapiens 0-16 21709601-2 2011 Heme oxygenase 2 (HMOX2) catalyzes the cleavage of the heme ring to form biliverdin with release of iron and carbon monoxide. Iron 100-104 heme oxygenase 2 Homo sapiens 18-23 21804464-5 2011 Heme oxygenase-2 is capable of degradation of heme producing free iron ions, thus, diversity in heme oxygenase-2 gene may contribute to AMD. Iron 66-70 heme oxygenase 2 Homo sapiens 0-16 21804464-5 2011 Heme oxygenase-2 is capable of degradation of heme producing free iron ions, thus, diversity in heme oxygenase-2 gene may contribute to AMD. Iron 66-70 heme oxygenase 2 Homo sapiens 96-112 17887916-3 2007 Physiologic heme degradation is catalyzed by two functional isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, yielding carbon monoxide, iron, and biliverdin, an immediate precursor to bilirubin. Iron 148-152 heme oxygenase 2 Homo sapiens 116-120 17408452-8 2007 HO (inducible HO-1, constitutive HO-2 and HO-3) is the rate-limiting enzyme in haeme catabolism, which leads to the generation of biliverdin, iron, and carbon monoxide. Iron 142-146 heme oxygenase 2 Homo sapiens 33-37 14562166-1 2003 INTRODUCTION: Heme oxygenase (HO) isoforms, HO-1, and HO-2, are responsible for heme breakdown to iron and carbon monoxide (CO). Iron 98-102 heme oxygenase 2 Homo sapiens 54-58 16787441-2 2006 Heme oxygenase consists of two structurally related isozymes, heme oxygenase-1 and and heme oxygenase-2, each of which cleaves heme to form biliverdin, iron and carbon monoxide. Iron 152-156 heme oxygenase 2 Homo sapiens 87-103 16601269-1 2006 The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO). Iron 262-266 heme oxygenase 2 Homo sapiens 81-85 14580148-2 2003 Heme degradation is catalyzed by the two isozymes of heme oxygenase, heme oxygenase-1 (HO-1) and HO-2, eventually yielding biliverdin/bilirubin, CO, and iron. Iron 153-157 heme oxygenase 2 Homo sapiens 97-101 12964953-5 2003 HO-1 and its constitutively expressed isozyme, heme oxygenase-2, catalyze the rate-limiting step in the conversion of heme to its metabolites, bilirubin IXalpha, ferrous iron, and carbon monoxide (CO). Iron 170-174 heme oxygenase 2 Homo sapiens 47-63 11554454-11 2001 Data suggest (a) each HRM can contribute to HO-2-heme interaction, (b) heme iron interacts with cysteine thiol, (c) charged residues upstream of Cys264-Pro265 result in its high-affinity heme binding, and (d) inhibition of HO-2 activity by synthetic metalloporphyrins does not involve HRMs. Iron 76-80 heme oxygenase 2 Homo sapiens 44-48 11554454-11 2001 Data suggest (a) each HRM can contribute to HO-2-heme interaction, (b) heme iron interacts with cysteine thiol, (c) charged residues upstream of Cys264-Pro265 result in its high-affinity heme binding, and (d) inhibition of HO-2 activity by synthetic metalloporphyrins does not involve HRMs. Iron 76-80 heme oxygenase 2 Homo sapiens 223-227 9468479-0 1998 Identification of histidine 45 as the axial heme iron ligand of heme oxygenase-2. Iron 49-53 heme oxygenase 2 Homo sapiens 64-80 9116047-1 1997 Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe. Iron 174-176 heme oxygenase 2 Homo sapiens 0-16 9116047-1 1997 Heme oxygenase-2 (HO-2) is constitutively expressed in mammalian tissues; together with HO-1 (HSP32) it catalyzes the cleavage of heme to produce biliverdin IX alpha, CO and Fe. Iron 174-176 heme oxygenase 2 Homo sapiens 18-22 35029613-6 2022 A core mechanism for the iron-catalyzed decomposition of H2O2 is proposed that is consistent with the principle of detailed balancing and includes both the one-electron oxidation of H2O2 by Fe(III) and the Fe(II) reduction of HO2 . Iron 25-29 heme oxygenase 2 Homo sapiens 226-229