PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
11258959-2	2001	GSH binding to MGST1 as measured by thiolate anion formation, proton release, and Meisenheimer complex formation is a slow process that can be described by a rapid binding step (K(GSH)d = 47 +/- 7 mM) of the peptide followed by slow deprotonation (k2 = 0.42 +/- 0.03 s(-1).	thiolate anion	36-50	microsomal glutathione S-transferase 1	Homo sapiens	15-20
11524005-1	2001	Most cytosolic glutathione S-transferases (GSTs) exploit a hydrogen bond between an active site Tyr and the bound glutathione (GSH) cofactor to lower the pK(a) of the GSH and generate the nucleophilic thiolate anion, GS(-).	thiolate anion	201-215	glutathione S-transferase alpha 1	Homo sapiens	43-47
17914842-9	2007	These data indicate that the gas-phase addition of a phosphine to the disulfide moiety will most likely form a phosphonium cation-thiolate anion salt, in the presence of four or more water molecules, that provide sufficient H-bonding stabilization to allow displacement of the thiolate anion, a normal uncomplicated SN2 transition state is to be expected.	thiolate anion	130-144	solute carrier family 38 member 5	Homo sapiens	316-319
12398152-8	2002	Under physiological conditions, thiyl radicals can react with thiolate anion yielding disulfide radical anion (RSSR)-* as an intermediate and finally disulfides and superoxide radical anion (O2-*), which is next inactivated in the reaction catalyzed by superoxide dismutase (SOD).	thiolate anion	62-76	superoxide dismutase 1	Homo sapiens	253-273
12398152-8	2002	Under physiological conditions, thiyl radicals can react with thiolate anion yielding disulfide radical anion (RSSR)-* as an intermediate and finally disulfides and superoxide radical anion (O2-*), which is next inactivated in the reaction catalyzed by superoxide dismutase (SOD).	thiolate anion	62-76	superoxide dismutase 1	Homo sapiens	275-278
10673221-7	2000	Also the Tyr-93 in LTC4 synthase has been suggested to function as a base for the formation of the thiolate anion of glutathione.	thiolate anion	99-113	leukotriene C4 synthase	Homo sapiens	19-32
10751412-1	2000	The glutathione S-transferase enzymes (GSTs) have a tyrosine or serine residue at their active site that hydrogen bonds to and stabilizes the thiolate anion of glutathione, GS(-).	thiolate anion	142-156	glutathione S-transferase alpha 2	Rattus norvegicus	39-43
9261869-5	1997	The functional implications of Tyr7 in the activation of the glutathione thiol group are discussed in the light of present results, which in agreement with previous studies suggest that Tyr7 in un-ionized form contributes to the catalytic process of glutathione S-transferase, the thiolate anion being stabilized by hydrogen bond with Tyr7 and by interactions with hydrating water molecules.	thiolate anion	281-295	glutathione S-transferase kappa 1	Homo sapiens	250-275
10384960-5	1999	The capability of the thiols to overcome their own inhibitory effect on CB was dependent on the concentration of their thiolate anion (RS-).	thiolate anion	119-133	cathepsin B	Homo sapiens	72-74
9153254-9	1997	These results suggest that in the catalytic function of LTC4S, Arg-51 probably opens the epoxide ring and Tyr-93 provides the thiolate anion of GSH.	thiolate anion	126-140	leukotriene C4 synthase	Homo sapiens	56-61
6098577-10	1984	Comparison of the EPR signal of oxidized H-450 with those of a cytochrome P-450, P-450(PB-1), and several model compounds indicated the presence of a thiolate anion at the 5th coordination position of the heme of H-450.	thiolate anion	150-164	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	63-79
8931546-4	1996	This thiolate anion is stabilized by 5.7 kcal/mol in the dithiol form, giving rise to the corresponding instability of the disulfide bond and the oxidizing properties of PDI a.	thiolate anion	5-19	prolyl 4-hydroxylase subunit beta	Homo sapiens	170-175
1761059-6	1991	Dimerization of fibronectin took place most effectively at pH greater than or equal to 8.8 but decreased strongly at lower pH, representing more unfavourable conditions for the action of the thiolate anion in the thiol/disulfide exchange reaction.	thiolate anion	191-205	fibronectin 1	Homo sapiens	16-27
2917017-3	1989	This spectrum indicates an interaction with the thiolate anion at cytochrome P-450; it can be blocked by previous addition of dithioerythritol.	thiolate anion	48-62	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	66-82
3044690-14	1988	While the active-site histidine of lipoamide dehydrogenase stabilizes the thiolate anion intermediate and relays a proton in the catalytic process.	thiolate anion	74-88	dihydrolipoamide dehydrogenase	Homo sapiens	35-58
6098577-10	1984	Comparison of the EPR signal of oxidized H-450 with those of a cytochrome P-450, P-450(PB-1), and several model compounds indicated the presence of a thiolate anion at the 5th coordination position of the heme of H-450.	thiolate anion	150-164	cytochrome P450, family 2, subfamily C, polypeptide 6, variant 1	Rattus norvegicus	81-91
2742854-0	1989	Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase.	thiolate anion	43-57	hematopoietic prostaglandin D synthase	Rattus norvegicus	95-120
2742854-1	1989	Ultraviolet difference spectroscopy of the binary complex of isozyme 4-4 of rat liver glutathione S-transferase with glutathione (GSH) and the enzyme alone or as the binary complex with the oxygen analogue, gamma-L-glutamyl-L-serylglycine (GOH), at neutral pH reveals an absorption band at 239 nm (epsilon = 5200 M-1 cm-1) that is assigned to the thiolate anion (GS-) of the bound tripeptide.	thiolate anion	347-361	hematopoietic prostaglandin D synthase	Rattus norvegicus	86-111
26755582-2	2016	Recently, a high-resolution crystal structure of human mPGES-1 was presented, with Ser-127 being proposed as the hydrogen-bond donor stabilizing thiolate anion formation within the cofactor, glutathione (GSH).	thiolate anion	145-159	prostaglandin E synthase	Mus musculus	55-62
681358-10	1978	The products of the model reaction and the covalently bound FAD of lipoamide dehydrogenase appear to be the result of a nucleophilic attack on the carbon at position 8 of the flavin ring by a thiolate anion, displacing the chloride.	thiolate anion	192-206	dihydrolipoamide dehydrogenase	Homo sapiens	67-90
7061465-2	1982	Evidence of several types has accumulated that cytochrome P-450 has a thiolate anion as one of the axial ligands to heme (the fifth ligand).	thiolate anion	70-84	cytochrome P-450	Oryctolagus cuniculus	47-63
7295776-2	1981	Reduced P-450SCC at pH 7.4 exhibited the V4 line at 1342 cm-1, which is an unusually low frequency compared with an ordinary protohemoprotein but is common to the family of cytochrome P-450, suggesting the coordination of a strong pi-donor such as thiolate anion at the fifth coordination position of the heme iron.	thiolate anion	248-262	cytochrome P450 family 11 subfamily A member 1	Homo sapiens	8-16
7295776-2	1981	Reduced P-450SCC at pH 7.4 exhibited the V4 line at 1342 cm-1, which is an unusually low frequency compared with an ordinary protohemoprotein but is common to the family of cytochrome P-450, suggesting the coordination of a strong pi-donor such as thiolate anion at the fifth coordination position of the heme iron.	thiolate anion	248-262	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	173-189
31590044-3	2020	The selenenyl anion of selenocysteine (Sec) is a stronger nucleophile, more prevalent at physiological pH, and more reactive than the corresponding thiolate anion of Cys.	thiolate anion	148-162	eukaryotic elongation factor, selenocysteine-tRNA-specific	Mus musculus	39-42
29390175-5	2018	The formation of a two-sulfur three-electron bonded disulfide radical anion (DRA) species by the reaction of a thiyl radical with a thiolate anion was determined as the cause for the reduction in catalytic radicals and the TEC rate.	thiolate anion	132-146	solute carrier family 26 member 3	Homo sapiens	77-80
19646993-5	2009	The enzymatic properties of MsrA indeed rely on the activation of the catalytic cysteine to the thiolate anion form that is potentially susceptible to oxidation by hydrogen peroxide.	thiolate anion	96-110	methionine sulfoxide reductase A	Homo sapiens	28-32
22219129-4	2012	Our data suggest that under normal circumstance, cysteine 111 residue in SOD1 is free; however, under oxidative stress, it is prone to oxidative modification by providing the thiolate anion (S-).	thiolate anion	175-189	superoxide dismutase 1	Homo sapiens	73-77
24338014-5	2014	From the crystal structure of plasminogen, we propose that plasmin ligands such as phosphoglycerate kinase induce a conformational change in reduced kringle 5 that leads to attack by the Cys(541) thiolate anion on the Cys(536) sulfur atom of the Cys(512)-Cys(536) disulfide bond, resulting in reduction of the bond by thiol/disulfide exchange.	thiolate anion	196-210	plasminogen	Homo sapiens	30-37
22217203-0	2012	Pre-steady-state kinetic characterization of thiolate anion formation in human leukotriene C4 synthase.	thiolate anion	45-59	leukotriene C4 synthase	Homo sapiens	79-102
22217203-8	2012	Taken together, these data establish that thiolate anion formation in hLTC4S is not the rate-limiting step for the overall reaction of LTC4 production (k(cat) = 26 s-1), and compared to the related microsomal glutathione transferase 1, which displays very slow GSH thiolate anion formation and one-third of the sites reactivity, hLTC4S has evolved a different catalytic mechanism.	thiolate anion	42-56	leukotriene C4 synthase	Homo sapiens	70-76
19658411-5	2009	The nu(Fe-CO) and nu(C-O) data reveal that the proximal heme ligand of iNOS(P420) is consistent with a protonated thiol instead of a thiolate anion.	thiolate anion	133-147	nitric oxide synthase 2	Homo sapiens	71-75