| Name | cytochrome c |
|---|---|
| Synonyms | CYC; CYCS; Cytochrome C; HCS; Cytochrome Cs |
| Name | ferrous sulfate |
|---|---|
| CAS | sulfuric acid iron(2+) salt (1:1) |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 18082361 | Ningappa MB, Srinivas L: Purification and characterization of approximately 35 kDa antioxidant protein from curry leaves (Murraya koenigii L.). Toxicol In Vitro. 2008 Apr;22(3):699-709. Epub 2007 Nov 17. In addition, APC reduced cytochrome c and ferric ion, chelated ferrous ion, and inhibited ferrous sulfate: -induced fragmentation and sugar oxidation to 80-90%. |
81(1,1,1,1) | Details |
| 184977 | Blayney L, Bailey-Wood R, Jacobs A, Henderson A, Muir J: The effects of iron deficiency on the respiratory function and cytochrome content of rat heart mitochondria. Circ Res. 1976 Nov;39(5):744-8. Both groups received identical diet but an iron supplement (180 mg of ferrous sulfate per kg of diet) was added for the control group. Isolated mitochondrial fractions from iron-deficient and control rats contained similar proportions of whole homogenate protein and succinic cytochrome c reductase activity, indicating that the fractions isolated from the experimental and control rats were comparable. |
2(0,0,0,2) | Details |
| 12675926 | Liu R, Liu W, Doctrow SR, Baudry M: toxicity in organotypic cultures of hippocampal slices: role of reactive species. J Neurochem. 2003 Apr;85(2):492-502. Exposure of mature hippocampal slices to ferrous sulfate resulted in concentration- and time-dependent cell death. Levels of cytochrome c were increased while levels of pro-caspase-9 and pro-caspase-3 were decreased in cytosolic fractions of iron-treated hippocampal slice cultures. |
2(0,0,0,2) | Details |
| 15752568 | Babizhayev MA, Semiletov YA, Lul'kin YA, Sakina NL, Savel'yeva EL, Alimbarova LM, Barinskii IP: 3D molecular modeling, free radical modulating and immune cells signaling activities of the novel peptidomimetic L-glutamyl- possible immunostimulating role. Peptides. 2005 Apr;26(4):551-63. Epub 2004 Dec 29. -Hist accelerated the decrease of ferrous iron in the ferrous sulfate solution in a concentration-dependent mode and showed the ferroxidase-like activity at concentrations less than 3 mM in the phenanthroline assay, whereas in the concentration range 3-20 mM -Hist restricted the availability of Fe2+ to phenanthroline due to binding of ferrous ions in chelating complexes. The stimulation of LPO by -Hist was related to the ability of peptidomimetic in small (approximately 0.05 mM) concentrations to release O2*- free radicals as determined by the superoxide dismutase-inhibitable cytochrome c reduction assay. |
1(0,0,0,1) | Details |
| 10381611 | Babizhayev MA, Semiletov YA, Lul'kin YA, Sakina NL, Savel'yeva EL, Deyev AI, Alimbarova LI, Barinskii IF, Nicolay J, Paillet C, Langrand G, Seguin F: Cellular signalling and free-radical modulating activities of the novel peptidomimetic L-glutamyl- Biochemistry. 1999 May;64(5):510-22. -Hist concentration-dependently accelerates a decrease in ferrous iron in ferrous sulfate solution and shows ferroxidase-like activity at concentrations less than 3 mM in the phenanthroline assay, whereas in the concentration range 3-20 mM it restricts the availability of Fe2+ to phenanthroline by chelation of iron ions. The stimulation of LPO by -Hist is related to its ability at low concentrations (*0.05 mM) to release O2 free radicals as determined by the superoxide dismutase-inhibitable reduction of cytochrome c. |
1(0,0,0,1) | Details |
| 6409153 | Brogan WC 3rd, Miles PR, Colby HD: Effects of lipid peroxidation on microsomal monooxygenases. . Biochim Biophys Acta. 1983 Jul 29;758(2):114-20. In addition, cytochrome P-450 levels, - and -cytochrome c reductase activities, and substrate interactions with cytochrome (s) P-450 decreased as lipid peroxidation progressed. |
1(0,0,0,1) | Details |
| 12013838 | Miki T: [Mitochondrial complex III -cytochrome c oxidoreductase)] Nippon Rinsho. 2002 Apr;60 Suppl 4:144-8. |
1(0,0,0,1) | Details |
| 15473686 | Kaneko M, Masui R, Ake K, Kousumi Y, Kuramitsu S, Yamaguchi M, Kuyama H, Ando E, Norioka S, Nakazawa T, Okamura TA, Yamamoto H, Ueyama N: Rapid and sensitive amino-acid sequencing of cloning Thermus thermophilus HB8 ferredoxin by proteomics. J Proteome Res. 2004 Sep-Oct;3(5):983-7. The catalytic electron-transfer reactivity of the [7Fe-8S] ferredoxin between ferredoxin- reductase and cytochrome c was recognized. |
1(0,0,0,1) | Details |