PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29354636-6 2017 In hIDO, by contrast, dioxygen must first coordinate to the heme iron because a bound substrate would occlude ligand access to the heme iron, so the ternary complex can no longer form. Iron 65-69 indoleamine 2,3-dioxygenase 1 Homo sapiens 3-7 29354636-6 2017 In hIDO, by contrast, dioxygen must first coordinate to the heme iron because a bound substrate would occlude ligand access to the heme iron, so the ternary complex can no longer form. Iron 136-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 3-7 25313323-2 2014 We report here the crystal structures of two IDO1/IDO1 inhibitor complexes, one of which shows that Amg-1 is directly bound to the heme iron of IDO1 with a clear induced fit. Iron 136-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 45-49 28412361-5 2017 INCB14943 binds to heme iron in IDO1 protein through the oxime nitrogen. Iron 24-28 indoleamine 2,3-dioxygenase 1 Homo sapiens 32-36 28963992-4 2017 UV-visible spectra study demonstrated that compounds 11p and 11r bound to IDO1 and coordinated with the heme iron. Iron 109-113 indoleamine 2,3-dioxygenase 1 Homo sapiens 74-78 28651980-1 2017 Docking studies of 4-phenylthiazolinethione on human IDO1 suggest complexation of the heme iron by the exocyclic sulfur atom further reinforced by hydrophobic interactions of the phenyl ring within pocket A of the enzyme. Iron 91-95 indoleamine 2,3-dioxygenase 1 Homo sapiens 53-57 25313323-2 2014 We report here the crystal structures of two IDO1/IDO1 inhibitor complexes, one of which shows that Amg-1 is directly bound to the heme iron of IDO1 with a clear induced fit. Iron 136-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 50-54 25313323-2 2014 We report here the crystal structures of two IDO1/IDO1 inhibitor complexes, one of which shows that Amg-1 is directly bound to the heme iron of IDO1 with a clear induced fit. Iron 136-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 50-54 11342657-6 2001 Similar to PDTC, the heme biosynthesis inhibitor succinylacetone (SA) and the iron-chelator pyridoxal isonicotinoyl hydrazone inhibited cellular IDO activity without affecting protein expression, whereas addition of hemin or the heme precursor delta-aminolevulinic acid increased IDO activity. Iron 78-82 indoleamine 2,3-dioxygenase 1 Homo sapiens 145-148 24939758-4 2014 The computational study of 3i suggested that the major interactions between 3i and IDO protein are the coordination of sulfone and heme iron, the hydrogen bonding and hydrophobic interactions between 3i and IDO. Iron 136-140 indoleamine 2,3-dioxygenase 1 Homo sapiens 83-86 21028817-4 2010 Binding of CO to l-Trp-bound IDO causes a significant change in the electronic and RR spectra of the heme, indicating that the pi* orbitals of the carbon atom of CO interact with pi orbitals of Fe and the porphyrin. Iron 194-196 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 16477023-6 2006 These characteristics of the IDO structure provide support for a reaction mechanism involving the abstraction of a proton from the substrate by iron-bound dioxygen. Iron 144-148 indoleamine 2,3-dioxygenase 1 Homo sapiens 29-32 21517759-4 2011 The active IDO conformer exists only in the presence of reducing cofactors (such as cytochrome b(5)), requiring the single electron reduction of ferric-to-ferrous iron (Fe(3+) Fe(2+)), which facilitates binding of L-Trp and O(2) to the enzyme active site. Iron 163-167 indoleamine 2,3-dioxygenase 1 Homo sapiens 11-14 18665584-4 2008 In particular, three interactions of 4-PI analogues with IDO were studied: the active site entrance, the interior of the active site, and the heme iron binding. Iron 147-151 indoleamine 2,3-dioxygenase 1 Homo sapiens 57-60 16420054-3 2006 Three important discoveries have been made, which will impact future IDO inhibitor development: (i) The dithiocarbamate portion of the brassinin lead is a crucial moiety, which may be binding to the heme iron of IDO; (ii) an indole ring is not necessary for IDO inhibition; and (iii) substitution of the S-methyl group of brassinin with large aromatic groups provides inhibitors that are three times more potent in vitro than the most commonly used IDO inhibitor, 1-methyl-tryptophan. Iron 204-208 indoleamine 2,3-dioxygenase 1 Homo sapiens 69-72 16420054-3 2006 Three important discoveries have been made, which will impact future IDO inhibitor development: (i) The dithiocarbamate portion of the brassinin lead is a crucial moiety, which may be binding to the heme iron of IDO; (ii) an indole ring is not necessary for IDO inhibition; and (iii) substitution of the S-methyl group of brassinin with large aromatic groups provides inhibitors that are three times more potent in vitro than the most commonly used IDO inhibitor, 1-methyl-tryptophan. Iron 204-208 indoleamine 2,3-dioxygenase 1 Homo sapiens 212-215 16420054-3 2006 Three important discoveries have been made, which will impact future IDO inhibitor development: (i) The dithiocarbamate portion of the brassinin lead is a crucial moiety, which may be binding to the heme iron of IDO; (ii) an indole ring is not necessary for IDO inhibition; and (iii) substitution of the S-methyl group of brassinin with large aromatic groups provides inhibitors that are three times more potent in vitro than the most commonly used IDO inhibitor, 1-methyl-tryptophan. Iron 204-208 indoleamine 2,3-dioxygenase 1 Homo sapiens 212-215 16420054-3 2006 Three important discoveries have been made, which will impact future IDO inhibitor development: (i) The dithiocarbamate portion of the brassinin lead is a crucial moiety, which may be binding to the heme iron of IDO; (ii) an indole ring is not necessary for IDO inhibition; and (iii) substitution of the S-methyl group of brassinin with large aromatic groups provides inhibitors that are three times more potent in vitro than the most commonly used IDO inhibitor, 1-methyl-tryptophan. Iron 204-208 indoleamine 2,3-dioxygenase 1 Homo sapiens 212-215 15109246-1 2004 Multiple-scattering analysis of X-ray absorption fine structure data on the NO adducts of indoleamine 2,3-dioxygenase (IDO) and analysis of X-ray absorption near-edge structure (XANES) have provided the first direct structural information about the iron center for this ubiquitous mammalian metalloprotein. Iron 249-253 indoleamine 2,3-dioxygenase 1 Homo sapiens 90-117 15109246-2 2004 The IDO(II)NO adduct, which is likely to play a physiological role in the immune system, differs from similar adducts such as Mb(II)NO and Lb(II)NO in that the Fe-His bond is essentially broken. Iron 160-162 indoleamine 2,3-dioxygenase 1 Homo sapiens 4-7 15109246-7 2004 The results indicate that both the blocking of the heme site to O(2) binding and conformational changes induced by breaking the Fe-N(epsilon) bond may be important mechanisms by which NO inhibits IDO in vitro and in vivo. Iron 128-132 indoleamine 2,3-dioxygenase 1 Homo sapiens 196-199 34242792-0 2021 Indoleamine 2, 3-dioxygenase 1 aggravates acetaminophen-induced acute liver failure by triggering excess nitroxidative stress and iron accumulation. Iron 130-134 indoleamine 2,3-dioxygenase 1 Homo sapiens 0-30 34242792-6 2021 In summary, our study confirmed that APAP-induced IDO1 aggravated ALF by triggering excess oxidative and nitrative stress and iron accumulation in liver. Iron 126-130 indoleamine 2,3-dioxygenase 1 Homo sapiens 50-54 33373218-4 2021 With X-ray crystallography, we detected an unexpected photochemical intermediate trapped in a crystal of the hIDO1-CO-Trp complex, where CO is photolyzed from the heme iron by X-rays at cryogenic temperatures (100 K). Iron 168-172 indoleamine 2,3-dioxygenase 1 Homo sapiens 109-114 33741464-4 2021 The molecular modeling of 19 with the X-ray crystal structure of IDO1 indicated that dipole-ionic interactions with heme iron, halogen bonding with Cys129 and the two hydrophobic interactions were important for the high potency of 19. Iron 121-125 indoleamine 2,3-dioxygenase 1 Homo sapiens 65-69 33101032-6 2020 The current study suggested that icotinib-1,2,3-triazole derivatives could be used as potential inhibitors that preferentially bind to the ferrous form of IDO1 through the formation of coordinate bond with the haem iron. Iron 215-219 indoleamine 2,3-dioxygenase 1 Homo sapiens 155-159