PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26649273-5	2015	This in vitro study extends earlier investigations of the oxidation of Arabidopsis cryptochrome1 by molecular oxygen and demonstrates that, under some conditions, a more complex model for oxidation of the flavin than was previously proposed is required to accommodate the spectral evidence (see P. Muller and M. Ahmad (2011) J. Biol.	Oxygen	110-116	cryptochrome 1	Arabidopsis thaliana	83-96	
25728686-3	2015	Recently, it has been shown that Arabidopsis cry1 activation by blue light also results in direct enzymatic conversion of molecular oxygen (O2 ) to reactive oxygen species (ROS) and hydrogen peroxide (H2 O2 ) in vitro.	Oxygen	132-138	cryptochrome 1	Arabidopsis thaliana	45-49	
25728686-3	2015	Recently, it has been shown that Arabidopsis cry1 activation by blue light also results in direct enzymatic conversion of molecular oxygen (O2 ) to reactive oxygen species (ROS) and hydrogen peroxide (H2 O2 ) in vitro.	Oxygen	140-142	cryptochrome 1	Arabidopsis thaliana	45-49	
26179959-3	2015	In a prior study, it has also been shown that Arabidopsis cry1 activation by blue light results in direct enzymatic conversion of molecular oxygen (O2) to ROS (reactive oxygen species) in vivo leading to cell death in overexpressing lines.	Oxygen	140-146	cryptochrome 1	Arabidopsis thaliana	58-62	
26179959-3	2015	In a prior study, it has also been shown that Arabidopsis cry1 activation by blue light results in direct enzymatic conversion of molecular oxygen (O2) to ROS (reactive oxygen species) in vivo leading to cell death in overexpressing lines.	Oxygen	148-150	cryptochrome 1	Arabidopsis thaliana	58-62	
21467031-4	2011	Here, we give evidence of a mechanism for the reverse reaction, namely dark reoxidation of protein-bound flavin in Arabidopsis thaliana cryptochrome (AtCRY1) by molecular oxygen that involves formation of a spin-correlated FADH( )-superoxide radical pair.	Oxygen	171-177	cryptochrome 1	Arabidopsis thaliana	150-156