PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31167903-4	2019	In the presence of the physiological electron acceptor cytochrome c, we were able to close the catalytic cycle of sulfite-dependent nitrite reduction thus leading to steady-state NO synthesis, a finding that strongly supports a physiological relevance of SO-dependent NO formation.	Sulfites	114-121	cytochrome c, somatic	Homo sapiens	55-67	
14729666-3	2004	In steady-state assays of Y343F sulfite oxidase using cytochrome c as the electron acceptor, k(cat) was somewhat impaired ( approximately 34% wild-type activity at pH 8.5), whereas the K(m)(sulfite) showed a 5-fold increase over wild type.	Sulfites	32-39	cytochrome c, somatic	Homo sapiens	54-66	
24793416-7	2014	Sulfite also induced mitochondrial swelling and reduced mitochondrial membrane potential, Ca(2+) retention capacity, NAD(P)H pool and cytochrome c immunocontent when Ca(2+) was present in the medium.	Sulfites	0-7	cytochrome c, somatic	Homo sapiens	134-146	
17009250-5	2006	After copper is added to the sulfite-cytochrome c binary systems, the reaction between sulfite and the protein component in cytochrome c is obviously strengthened at a low concentration (K(A) = 7.289 L mol(-1)), while the addition of copper merely has a little effect on the interaction between sulfite and the ferroporphyrin component in cytochrome c.	Sulfites	29-36	cytochrome c, somatic	Homo sapiens	37-49	
17009250-5	2006	After copper is added to the sulfite-cytochrome c binary systems, the reaction between sulfite and the protein component in cytochrome c is obviously strengthened at a low concentration (K(A) = 7.289 L mol(-1)), while the addition of copper merely has a little effect on the interaction between sulfite and the ferroporphyrin component in cytochrome c.	Sulfites	29-36	cytochrome c, somatic	Homo sapiens	124-136	
17009250-5	2006	After copper is added to the sulfite-cytochrome c binary systems, the reaction between sulfite and the protein component in cytochrome c is obviously strengthened at a low concentration (K(A) = 7.289 L mol(-1)), while the addition of copper merely has a little effect on the interaction between sulfite and the ferroporphyrin component in cytochrome c.	Sulfites	29-36	cytochrome c, somatic	Homo sapiens	124-136	
17009250-5	2006	After copper is added to the sulfite-cytochrome c binary systems, the reaction between sulfite and the protein component in cytochrome c is obviously strengthened at a low concentration (K(A) = 7.289 L mol(-1)), while the addition of copper merely has a little effect on the interaction between sulfite and the ferroporphyrin component in cytochrome c.	Sulfites	87-94	cytochrome c, somatic	Homo sapiens	37-49	
17009250-5	2006	After copper is added to the sulfite-cytochrome c binary systems, the reaction between sulfite and the protein component in cytochrome c is obviously strengthened at a low concentration (K(A) = 7.289 L mol(-1)), while the addition of copper merely has a little effect on the interaction between sulfite and the ferroporphyrin component in cytochrome c.	Sulfites	87-94	cytochrome c, somatic	Homo sapiens	124-136	
17009250-5	2006	After copper is added to the sulfite-cytochrome c binary systems, the reaction between sulfite and the protein component in cytochrome c is obviously strengthened at a low concentration (K(A) = 7.289 L mol(-1)), while the addition of copper merely has a little effect on the interaction between sulfite and the ferroporphyrin component in cytochrome c.	Sulfites	87-94	cytochrome c, somatic	Homo sapiens	124-136	
26709389-9	2016	Studies were performed to understand the related mechanism of oxidation of sulfite and radical generation by ferric cytochrome c (Fe3+ cyt c) in the absence and presence of H2O2.	Sulfites	75-82	cytochrome c, somatic	Homo sapiens	116-128	
26709389-9	2016	Studies were performed to understand the related mechanism of oxidation of sulfite and radical generation by ferric cytochrome c (Fe3+ cyt c) in the absence and presence of H2O2.	Sulfites	75-82	cytochrome c, somatic	Homo sapiens	135-140	
26709389-12	2016	The amount of DMPO-SO3- formed from the oxidation of sulfite by the Fe3+ cyt c increased with sulfite concentration.	Sulfites	53-60	cytochrome c, somatic	Homo sapiens	73-78	
26709389-12	2016	The amount of DMPO-SO3- formed from the oxidation of sulfite by the Fe3+ cyt c increased with sulfite concentration.	Sulfites	94-101	cytochrome c, somatic	Homo sapiens	73-78	
26709389-13	2016	In addition, the amount of DMPO-SO3- formed by the peroxidase activity of Fe3+ cyt c also increased with sulfite and H2O2 concentration.	Sulfites	105-112	cytochrome c, somatic	Homo sapiens	79-84	
26709389-14	2016	From these results, we propose a mechanism in which the Fe3+ cyt c and its peroxidase activity oxidizes sulfite to sulfite radical.	Sulfites	104-111	cytochrome c, somatic	Homo sapiens	61-66	
26709389-15	2016	Our results suggest that Fe3+ cyt c could have a novel role in the deleterious effects of sulfite in biological systems due to increased production of sulfite radical.	Sulfites	90-97	cytochrome c, somatic	Homo sapiens	30-35	
18932024-0	2009	Electrocatalytic sulfite biosensor with human sulfite oxidase co-immobilized with cytochrome c in a polyelectrolyte-containing multilayer.	Sulfites	17-24	cytochrome c, somatic	Homo sapiens	82-94	
17320039-5	2007	In hypotonic medium, magnesium and potassium ions have a protective effect on the release of enzymes and on the reactivity of cyto-c as electron acceptor from both sulfite and succinate; results which are consistent with the view that MOM preserves its identity and remains not permeable to exogenous cyto-c.	Sulfites	164-171	cytochrome c, somatic	Homo sapiens	126-132