PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
27089923-6	2016	We examine the heme-binding pockets and explore the versatility of the alpha + beta barrels ability to accommodate heme or heme-related moieties, such as siroheme, in at least three different sites, namely, the mode seen in IsdG/OxdA, Cld/DyP/EfeB/HemQ and siroheme decarboxylase barrels.	Heme	115-119	D-amino acid oxidase	Homo sapiens	229-233	
27089923-5	2016	Our comparative structural analysis of these heme-binding barrels reveals two distinct modes of packing of the ferredoxin-like domains to constitute the alpha + beta barrel, which is typified by the Type-1/IsdG-like and Type-2/OxdA-like proteins, respectively.	Heme	45-49	D-amino acid oxidase	Homo sapiens	227-231	
27089923-6	2016	We examine the heme-binding pockets and explore the versatility of the alpha + beta barrels ability to accommodate heme or heme-related moieties, such as siroheme, in at least three different sites, namely, the mode seen in IsdG/OxdA, Cld/DyP/EfeB/HemQ and siroheme decarboxylase barrels.	Heme	115-119	D-amino acid oxidase	Homo sapiens	229-233	
15339918-6	2004	These findings suggest that His(320) is located in the distal heme pocket of OxdA and would donate a proton to the substrate in the aldoxime dehydration mechanism.	Heme	62-66	D-amino acid oxidase	Homo sapiens	77-81	
23382199-2	2013	Unlike the utilization of H(2)O(2) or O(2) as a mediator of catalysis by other heme-containing enzymes (e.g., P450), OxdA is notable for the direct binding of a substrate to the heme iron.	Heme	79-83	D-amino acid oxidase	Homo sapiens	117-121	
23382199-2	2013	Unlike the utilization of H(2)O(2) or O(2) as a mediator of catalysis by other heme-containing enzymes (e.g., P450), OxdA is notable for the direct binding of a substrate to the heme iron.	Heme	178-182	D-amino acid oxidase	Homo sapiens	117-121	
23382199-4	2013	We then constructed OxdA mutants in which each of the polar amino acids lying within ~6 A of the iron atom of the heme was converted to alanine.	Heme	114-118	D-amino acid oxidase	Homo sapiens	20-24	
15196918-1	2004	Resonance Raman spectra have been measured to characterize the heme environment in aldoxime dehydratase (OxdA), a novel hemoprotein, which catalyzes the dehydration of aldoxime into nitrile.	Heme	63-67	D-amino acid oxidase	Homo sapiens	105-109