Isolated noncatalytic and catalytic subunits of F1-ATPase exhibit similar, albeit not identical, energetic strategies for recognizing adenosine nucleotides.
Biochim Biophys Acta
; 1837(1): 44-50, 2014 Jan.
Article
en En
| MEDLINE
| ID: mdl-23994287
Palabras clave
2-amino-2-(hydroxymethyl)propane-1,3-diol; ADP; ATP; ATPase; Binding energetics; EDTA; EF1; F(1)-ATPase; F1 sector from Bacillus PS3; F1 sector from Escherichia coli; Heterotropic cooperativity; ITC; Isolated subunit; Isothermal titration calorimetry; K(N1) and K(N2); K(Pf) and K(Pb); K(b); K(d); Metal binding; Mg(II); MgCl2; NMR; S1, S2 and S3; TF1; Tris; adenosine 5'-diphosphate; adenosine 5'-triphosphatase; adenosine 5'-triphosphate; association constants for ATP and Mg·ATP binding to the subunit; binding Gibbs free energy; binding enthalpy; binding entropy; cooperative Gibbs free energy; cooperative enthalpy; cooperative entropy; cooperative heterotropic association constant; equilibrium binding constant; equilibrium dissociation constant; ethylenediaminetetraacetic acid; free magnesium ion; high, medium and low affinity ß-subunit sites in F1, respectively; isothermal titration calorimetry; magnesium chloride; nuclear magnetic resonance; step-wise association constants for the interaction of ATP with Mg(II); ΔG(b); ΔH(b); ΔS(b); Δg; Δh; Δs; ß subunits in the crystal structure of F1 bound to Mg·ADP and Mg·AMPPNP, respectively; ßDP and ßTP; κ
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Adenosina
/
ATPasas de Translocación de Protón
/
Dominio Catalítico
/
Metabolismo Energético
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
2014
Tipo del documento:
Article
País de afiliación:
México