| Name | myoglobin |
|---|---|
| Synonyms | MB; Myoglobin; PVALB; Myoglobins |
| Name | rotenone |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 1858930 | Doeller JE, Wittenberg BA: Myoglobin function and energy metabolism of isolated cardiac myocytes: effect of Am J Physiol. 1991 Jul;261(1 Pt 2):H53-62. However, inhibition of electron transport by rotenone does block myoglobin-mediated uptake. |
86(1,1,1,6) | Details |
| 9067905 | Zager RA, Burkhart K: Myoglobin toxicity in proximal human kidney cells: roles of Fe, Ca2+, H2O2, and terminal mitochondrial electron transport. Kidney Int. 1997 Mar;51(3):728-38. Blockade of site 2 (antimycin) and site 3 (azide), but not site 1 (rotenone), mitochondrial electron transport significantly reduced myoglobin cytotoxicity. |
6(0,0,0,6) | Details |
| 19178274 | Ramanathan R, Mancini RA, Konda MR: Effects of lactate on beef heart mitochondrial consumption and muscle darkening. J Agric Food Chem. 2009 Feb 25;57(4):1550-5. Rotenone reduced (p < 0.05) lactate-mediated darkening in bovine cardiac muscle homogenates. Lactate-induced beef color darkening may be due to increased consumption by mitochondria, which out-competes myoglobin for and results in dark colored muscle. |
1(0,0,0,1) | Details |
| 5062477 | Wu CS, Duffy P, Brown WD: Interaction of myoglobin and cytochrome C. J Biol Chem. 1972 Mar 25;247(6):1899-903. |
1(0,0,0,1) | Details |
| 15969532 | Tang J, Faustman C, Mancini RA, Seyfert M, Hunt MC: Mitochondrial reduction of metmyoglobin: dependence on the electron transport chain. J Agric Food Chem. 2005 Jun 29;53(13):5449-55. Reduction of ferric myoglobin (metmyoglobin, MetMb) to its ferrous form is important for maintaining fresh meat color because only reduced myoglobin can bind to form the consumer-preferred cherry red color in fresh meat. MetMb reduction was increased by rotenone addition and decreased by (p < 0.05); the reduction was completely abolished by additions of antimycin A or myxothiazol when compared with controls (p < 0.05). |
1(0,0,0,1) | Details |
| 14713113 | Gnaiger E: conformance of cellular respiration. Adv Exp Med Biol. 2003;543:39-55. In cultured cells, the pronounced uptake above mitochondrial saturation at air-level pressure cannot be inhibited by rotenone and antimycin A, amounting to > 20 % of routine respiration in fibroblasts. Thus mitochondrial respiration proceeds at 90% of its hyperbolic maximum at the p50 of myoglobin, suggesting the possibility of a small but significant limitation even under normoxia in active muscle. |
1(0,0,0,1) | Details |