The pathway for spontaneous occlusion of Rb+ in the Na +/K+-ATPase
Occlusion of K+ in the Na+/K+-ATPase can be achieved under two conditions: during hydrolysis of ATP, in media with Na+ and Mg2+, after the K+-stimulated dephosphorylation of E2P (physiological route) or spontaneously, after binding of K+ to the enzyme (direct route). We investigated the sidedness of...
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2008
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 08625caa a22010337a 4500 | ||
|---|---|---|---|
| 001 | PAPER-22387 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518205356.0 | ||
| 008 | 190411s2008 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-44449137625 | |
| 024 | 7 | |2 cas |a adenosine triphosphate, 15237-44-2, 56-65-5, 987-65-5; magnesium ion, 22537-22-0; phosphate, 14066-19-4, 14265-44-2; potassium ion, 24203-36-9; rubidium ion, 22537-38-8; sodium ion, 17341-25-2; Ligands; Magnesium, 7439-95-4; Potassium, 7440-09-7; Rubidium, 7440-17-7; Sodium, 7440-23-5; Sodium-Potassium-Exchanging ATPase, EC 3.6.3.9 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a BICHA | ||
| 100 | 1 | |a González-Lebrero, R.M. | |
| 245 | 1 | 4 | |a The pathway for spontaneous occlusion of Rb+ in the Na +/K+-ATPase |
| 260 | |c 2008 | ||
| 270 | 1 | 0 | |m Rossi, R. C.; Instituto de Química Y Fisicoquímica Biológicas, Departamento de Química Biológica, Universidad de Buenos Aires, Junín 956, C1113AAD, Buenos Aires, Argentina; email: rcr@mail.retina.ar |
| 506 | |2 openaire |e Política editorial | ||
| 504 | |a Morth, J.P., Pedersen, B.P., Toustrup-Jensen, M.S., Sørensen, T.L., Petersen, J., Andersen, J.P., Vilsen, B., Nissen, P., Crystal structure of the sodium-potassium pump (2007) Nature, 450, pp. 1043-1049 | ||
| 504 | |a Beaugé, L.A., Glynn, I.M., Occlusion of K ions in the unphosphorylated sodium pump (1979) Nature, 280, pp. 510-512 | ||
| 504 | |a Forbush III, B., An apparatus for rapid kinetic analysis of isotopic efflux from membrane vesicles and of ligand dissociation from membrane proteins (1984) Anal. Biochem, 140, pp. 495-505 | ||
| 504 | |a Rossi, R.C., Kaufman, S.B., González-Lebrero, R.M., Nørby, J.G., Garrahan, P.J., An attachment for nondestructive, fast quenching of samples in rapid-mixing experiments (1999) Anal. Biochem, 270, pp. 276-285 | ||
| 504 | |a González-Lebrero, R.M., Kaufman, S.B., Montes, M.R., Nørby, J.G., Garrahan, P.J., Rossi, R.C., The occlusion of Rb+ in the Na+/K+-ATPase. I. The identity of occluded states formed by the physiological or the direct routes: Occlusion/deocclusion kinetics through the direct route (2002) J. Biol. Chem, 277, pp. 5910-5921 | ||
| 504 | |a Forbush, B., III (1988) Overview: occluded ions and Na, K-ATPase, in The Na+,K+-Pump. Part A, Molecular Aspects (Skou, J. C., Nørby J. G., Maunsbach, A. B., and Esmann M., Eds.) pp 229-248, Alan Liss, Inc., New York; Karlish, S.J.D., Stein, W.D., Passive rubidium fluxes mediated by Na-K-ATPase reconstituted into phospholipid vesicles when ATP- and phosphate-free (1982) J. Physiol, 328, pp. 295-316 | ||
| 504 | |a Forbush III, B., Rapid release of 42K or 86Rb from two distinct transport sites on the Na,K-pump in the presence of Pi or vanadate (1987) J. Biol. Chem, 262, pp. 11116-11127 | ||
| 504 | |a Glynn, I.M., Howland, J.L., Richards, D.E., Evidence for the ordered release of rubidium ions occluded within the Na,K-ATPase of mammalian kidney (1985) J. Physiol, 368, pp. 453-469 | ||
| 504 | |a González-Lebrero, R.M., Kaufman, S.B., Garrahan, P.J., Rossi, R.C., The sidedness of the direct route of occlusion of K + in the Na+/K+-ATPase (2003) Ann. N.Y. Acad. Sci, 986, pp. 301-303 | ||
| 504 | |a Jensen, J., Nørby, J.G., Ottolenghi, P., Binding of sodium and potassium to the sodium pump of pig kidney evaluated from nucleotide-binding behaviour (1984) J. Physiol. (London), 346, pp. 219-241 | ||
| 504 | |a Burnham, K.P., Anderson, D.R., (2002) Model Selection and Multimodel Inference, pp. 60-85. , 2nd ed, pp, Springer, New York | ||
| 504 | |a Fraser, R.D.B., Suzuki, E., The use of least squares in data analysis (1973) Physical Principles and Techniques of Protein Chemistry: Part C, pp. 301-355. , Leach, S. J, Ed, pp, Academic Press, New York | ||
| 504 | |a González-Lebrero, R.M., (2001) Caracterización cinética del fenómeno de oclusión de K+ en la Na+/K+-ATPasa, , Ph.D. thesis, University of Buenos Aires | ||
| 504 | |a Glynn, I.M., Karlish, S.J.D., Occluded cations in active transport (1990) Annu. Rev. Biochem, 59, pp. 171-205 | ||
| 504 | |a Fedosova, N.U., Esmann, M., Nucleotide-binding kinetics of Na,K-ATPase: Cation dependence (2004) Biochemistry, 43, pp. 4212-4218 | ||
| 504 | |a González-Lebrero, R.M., Kaufman, S.B., Garrahan, P.J., Rossi, R.C., The occlusion of Rb+ in the Na+/K +-ATPase. II. The effects of Rb+, Na+, Mg 2+ or ATP on the equilibrium between free and occluded Rb + (2002) J. Biol. Chem, 277, pp. 5922-5928 | ||
| 504 | |a Karlish, S.J., Pick, U., Sidedness of the effects of sodium and potassium ions on the conformational state of the sodium-potassium pump (1981) J. Physiol, 312, pp. 505-529 | ||
| 504 | |a Jørgensen, P.L., Håkansson, K.O., Karlish, S.J., Structure and mechanism of Na,K-ATPase: Functional sites and their interactions (2003) Annu. Rev. Physiol, 65, pp. 817-849 | ||
| 520 | 3 | |a Occlusion of K+ in the Na+/K+-ATPase can be achieved under two conditions: during hydrolysis of ATP, in media with Na+ and Mg2+, after the K+-stimulated dephosphorylation of E2P (physiological route) or spontaneously, after binding of K+ to the enzyme (direct route). We investigated the sidedness of spontaneous occlusion and deocclusion of Rb+ in an unsided, purified preparation of Na+/K+-ATPase. Our studies were based on two propositions: (i) in the absence of ATP, deocclusion of K+ and its congeners is a sequential process where two ions are released according to a single file mechanism, both in the absence and in the presence of Mg 2+ plus inorganic orthophosphate (Pi), and (ii) in the presence of Mg2+ plus Pi, exchange of K+ would take place through sites exposed to the extracellular surface of the membrane. The experiments included a double incubation sequence where one of the two Rb+ ions was labeled as 86Rb+. We found that, when the enzyme is in the E2 conformation, the first Rb+ that entered the enzyme in media without Mg2+ and Pi was the last to leave after addition of Mg 2+ plus Pi, and vice-versa. This indicates that spontaneous exchange of Rb+ between E2(Rb2) and the medium takes place when the transport sites are exposed to the extracellular surface of the membrane. Our results open the question if occlusion and deocclusion via the direct route participates in any significant degree in the transport of K+ during the ATPase activity. © 2008 American Chemical Society. |l eng | |
| 593 | |a Instituto de Química Y Fisicoquímica Biológicas, Departamento de Química Biológica, Universidad de Buenos Aires, Junín 956, C1113AAD, Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a ADENOSINETRIPHOSPHATE |
| 690 | 1 | 0 | |a ENZYME ACTIVITY |
| 690 | 1 | 0 | |a POSITIVE IONS |
| 690 | 1 | 0 | |a RUBIDIUM |
| 690 | 1 | 0 | |a SODIUM |
| 690 | 1 | 0 | |a DEOCCLUSION |
| 690 | 1 | 0 | |a INCUBATION SEQUENCES |
| 690 | 1 | 0 | |a TRANSPORT SITES |
| 690 | 1 | 0 | |a ENZYME KINETICS |
| 690 | 1 | 0 | |a ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM) |
| 690 | 1 | 0 | |a ADENOSINE TRIPHOSPHATE |
| 690 | 1 | 0 | |a KIDNEY ENZYME |
| 690 | 1 | 0 | |a MAGNESIUM ION |
| 690 | 1 | 0 | |a PHOSPHATE |
| 690 | 1 | 0 | |a POTASSIUM ION |
| 690 | 1 | 0 | |a RUBIDIUM ION |
| 690 | 1 | 0 | |a SODIUM ION |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CELL MEMBRANE |
| 690 | 1 | 0 | |a CELL SURFACE |
| 690 | 1 | 0 | |a DEPHOSPHORYLATION |
| 690 | 1 | 0 | |a ENZYME ACTIVITY |
| 690 | 1 | 0 | |a ENZYME CONFORMATION |
| 690 | 1 | 0 | |a HYDROLYSIS |
| 690 | 1 | 0 | |a ION TRANSPORT |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a SWINE |
| 690 | 1 | 0 | |a ANIMALS |
| 690 | 1 | 0 | |a BINDING SITES |
| 690 | 1 | 0 | |a KIDNEY |
| 690 | 1 | 0 | |a KINETICS |
| 690 | 1 | 0 | |a LIGANDS |
| 690 | 1 | 0 | |a MAGNESIUM |
| 690 | 1 | 0 | |a POTASSIUM |
| 690 | 1 | 0 | |a RUBIDIUM |
| 690 | 1 | 0 | |a SODIUM |
| 690 | 1 | 0 | |a SODIUM-POTASSIUM-EXCHANGING ATPASE |
| 690 | 1 | 0 | |a SWINE |
| 700 | 1 | |a Kaufman, S.B. | |
| 700 | 1 | |a Garrahan, P.J. | |
| 700 | 1 | |a Rossi, R.C. | |
| 773 | 0 | |d 2008 |g v. 47 |h pp. 6073-6080 |k n. 22 |p Biochemistry |x 00062960 |w (AR-BaUEN)CENRE-755 |t Biochemistry | |
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| 856 | 4 | 0 | |u https://doi.org/10.1021/bi800270k |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_00062960_v47_n22_p6073_GonzalezLebrero |y Handle |
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