| Name | proton pump |
|---|---|
| Synonyms | ATP12A; Cation transporting ATPase; Proton pump; ATP12A protein; ATP1AL1; Non gastric H(+)/K(+) ATPase subunit alpha; Non gastric H+/K+ ATPase alpha subunit; Potassium transporting ATPase alpha chain 2… |
| Name | rotenone |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 39598 | Krab K, Wikstrom M: On the stoichiometry and thermodynamics of -pumping cytochrome c oxidase in mitochondria. Biochim Biophys Acta. 1979 Oct 10;548(1):1-15. Similar results are obtained with either ferrocyanide, N.N.N',N'-tetramethyl-p-phenylenediamine or externally added cytochrome c mediating between and cytochrome c in rotenone- and antimycin-inhibited mitochondria. These results provide strong evidence that cytochrome c oxidase functions as a redox-linked proton pump with a stoichiometry of one H+ ejected and two charges translocated/electron transferred. |
2(0,0,0,2) | Details |
| 2862915 | Herweijer MA, Berden JA, Kemp A, Slater EC: Inhibition of energy-transducing reactions by 8-nitreno-ATP covalently bound to bovine heart submitochondrial particles: direct interaction between ATPase and redox enzymes. Biochim Biophys Acta. 1985 Aug 28;809(1):81-9. In reversal, where ATPase functions as primary proton pump, inactivation by covalently bound nitreno-ATP results in an inhibition that is proportional to the inactivation of ATP hydrolysis, or, consequently, with the concentration of inactivated ATP synthases. Inhibition of one of the primary pumps of -driven ATP synthesis, the NADH:Q oxidoreductase, with rotenone also resulted in an inhibition of the rate of ATP synthesis proportional to that of the oxidation. |
2(0,0,0,2) | Details |
| 1587679 | Gozar MM, O'Sullivan WJ, Bagnara AS: Mitochondrial function in Babesia bovis. Int J Parasitol. 1992 Apr;22(2):165-71. However, those drugs that were found to inhibit babesial growth included compounds (shown in parentheses) that have the following putative mitochondrial targets in the parasite: ATP synthetase complex (rhodamine 123, oligomycin, Janus Green); ATP-ADP translocase (bongkrekic acid); electron transport (rotenone, n-heptyl-4-hydroxyquinoline-N-oxide (HQNO), antimycin A); function (BW58C, menoctone); protein synthesis (tetracycline); and the proton pump (CCCP). |
81(1,1,1,1) | Details |
| 2314 | Azzone GF, Massair S, Pozzan T: Mechanism of active shrinkage in mitochondria. Biochim Biophys Acta. 1976 Jan 15;423(1):27-41. Three models of active shrinkage are discussed: (a) mechanoprotein, (b) electrogenic proton pump, and (c) -driven cation anion pump. |
1(0,0,0,1) | Details |
| 4052077 | Barr R, Sandelius AS, Crane FL, Morre DJ: Oxidation of reduced nucleotides by plasma membranes of soybean hypocotyl. Biochem Biophys Res Commun. 1985 Sep 16;131(2):943-8. The function of this enzyme is unknown at present, but it may represent a redox-controlled proton pump linked to acidification. |
1(0,0,0,1) | Details |
| 6619770 | Working PK, Meizel S: Correlation of increased intraacrosomal pH with the hamster sperm acrosome reaction. J Exp Zool. 1983 Jul;227(1):97-107. The results of this and previous studies lead us to suggest here that the intraacrosomal pH rise may be mediated via a change in K+ and H+ permeability of sperm head membranes, which allows K+ influx and H+ efflux, and via inhibition of an acrosomal Mg2+-ATPase proton pump. Addition of the mitochondrial electron transport inhibitor rotenone (2.5 microM) at 3.5 hr or of NaCl (3 mM) or KCl (3 mM) at 4 hr did not stimulate AR over control levels, suggesting that the stimulation of AR by the other compounds was not directly due to depletion of acrosomal (ATP) or alteration of the acrosomal transmembrane potential. |
1(0,0,0,1) | Details |
| 19961238 | Shinzawa-Itoh K, Seiyama J, Terada H, Nakatsubo R, Naoki K, Nakashima Y, Yoshikawa S: Bovine heart NADH-ubiquinone oxidoreductase contains one molecule of with ten isoprene units as one of the cofactors. Biochemistry. 2010 Jan 26;49(3):487-92. The rotenone-sensitive enzymatic activity of the Complex I preparation was comparable to that of Complex I in the mitochondrial membrane. It has been proposed that Complex I has two Q (10) binding sites, one involved in the proton pump and the other functioning as a converter between one and two electron transfer pathways [Ohnishi, T., Johnson, J. |
1(0,0,0,1) | Details |
| 10762084 | Chinopoulos C, Tretter L, Adam-Vizi V: Reversible depolarization of in situ mitochondria by oxidative stress parallels a decrease in NAD (P) H level in nerve terminals. Neurochem Int. 2000 May;36(6):483-8. Neurochem. 73, 220 228) that mitochondrial membrane potential (delta (psi) m) in isolated nerve terminals is markedly reduced by H2O2 in the absence of F0F1-ATPase working as a proton pump. The effect of H2O2 on delta (psi) m in the presence of the complex I inhibitor, rotenone, was also unaltered by addition of catalase. |
1(0,0,0,1) | Details |
| 1645458 | Bienen EJ, Saric M, Pollakis G, Grady RW, Clarkson AB Jr: Mitochondrial development in Trypanosoma brucei brucei transitional bloodstream forms. Mol Biochem Parasitol. 1991 Apr;45(2):185-92. The EMF is inhibited by 2,4-dinitrophenol, rotenone and salicylhydroxamic acid but not by antimycin A or This putative production is either by F1F0 ATPase driven by the complex I proton pump or by mitochondrial substrate level phosphorylation, or most likely by both. |
1(0,0,0,1) | Details |
| 6603696 | Bulychev AG, Veselkina MN: [Effect of inhibitors of energy metabolism and protein synthesis on the process of neutral red segregation in frog erythrocytes]. Tsitologiia. 1983 Apr;25(4):426-33. The fact that low concentrations of FCCP and DNP inhibit the process of segregation brings a supporting evidence for the possibility of the ATP-driven proton pump involved in Neutral red segregation. This influence was most striking with antimycin A, rotenone and |
1(0,0,0,1) | Details |
| 2421768 | Herweijer MA, Berden JA, Slater EC: Uncoupler-inhibitor titrations of ATP-driven reverse electron transfer in bovine submitochondrial particles provide evidence for direct interaction between ATPase and NADH:Q oxidoreductase. Biochim Biophys Acta. 1986 Apr 24;849(2):276-87. Contrary to this prediction several uncouplers (S13, SF6847, 2,4-dinitrophenol, valinomycin + nigericin) show an increase in uncoupling efficiency in ATP-driven reverse electron transfer (reversal) upon inhibition of the secondary pump in this reaction, the NADH:Q oxidoreductase, by rotenone. |
0(0,0,0,0) | Details |