PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11148040-5	2001	In this study, we have characterized the heme cofactor of CBS in both the ferric and ferrous states using resonance Raman spectroscopy.	Ferric enterobactin ion	74-80	cystathionine beta-synthase	Homo sapiens	58-61	
20155941-4	2010	Normal coordinate structural decomposition (NSD) of the ferric CBS crystal structure predicts the enhancement of normal modes with significant heme "doming", "ruffling", and "saddling" content, and they are observed in the coherence spectra near approximately 40, approximately 60, and approximately 90 cm(-1).	Ferric enterobactin ion	56-62	cystathionine beta-synthase	Homo sapiens	63-66	
21875066-2	2011	The presence of a heme cofactor in CBS is enigmatic, and its conversion from the ferric- to ferrous-CO state inhibits enzyme activity.	Ferric enterobactin ion	81-87	cystathionine beta-synthase	Homo sapiens	35-38	
20155941-6	2010	For ferric CBS, we observe a new mode near approximately 25 cm(-1), possibly involving the response of the protein, which exhibits a phase jump of approximately pi for excitation on the blue and red side of the Soret band maximum.	Ferric enterobactin ion	4-10	cystathionine beta-synthase	Homo sapiens	11-14	
15544339-5	2004	Instead, pH was found to control the equilibrium amount of ferric and ferrous heme present after reaction of CBS with one-electron reducing agents.	Ferric enterobactin ion	59-65	cystathionine beta-synthase	Homo sapiens	109-112