PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18821763-4	2008	Analysis of the kinetics of the reaction at 28 mM water indicates that second order rate constant for the catalytic reaction, given as kcatmax/Kd, is 4.6 x 104 M(-1) s(-1), is a factor of 8.4 x 10(10) larger than the second order rate constant (k2EtO) for the ethoxide promoted reaction of 2 in ethanol (5.5 +/- 0.3) x 10(-7) M(-1) s(-1).	Water	50-55	RUNX1 partner transcriptional co-repressor 1	Homo sapiens	247-250	
16961363-3	2006	The extent of a structural change of the iron center from a preferred square-pyramidal to a distorted trigonal-bipyramidal geometry varies with the external ligand that is bound in the order Cl << EtO < H2O, which is consistent with the spectrochemical series.	Water	212-215	RUNX1 partner transcriptional co-repressor 1	Homo sapiens	203-206	
17256929-3	2007	In the presence of the triaza ligand:Zn2+ complex, the change from water to methanol and then to ethanol brings about a mechanism where two molecules of the complex, suggested as EtOH:Zn2+:[12]aneN3 and its basic form, EtO-:Zn2+:[12]aneN3, bind to HPNPP and catalyze its decomposition with a rate constant of kcat of 0.13 s(-1) at s(s)pH 7.1.	Water	67-72	RUNX1 partner transcriptional co-repressor 1	Homo sapiens	179-182	
16268581-5	2005	Addition of ethanol, water, or pyrrole converts {[(H)OCPH]H3]2+ into [(H,EtO)OCPH]H2, [(H,OH)OCPH]H2, or pyrrole appended O-confused porphyrin [(H,pyrrole)OCPH]H2, respectively.	Water	21-26	RUNX1 partner transcriptional co-repressor 1	Homo sapiens	73-76