Metal ion binding to adenosine triphosphate. III. Kinetic analysis

Sternlicht, H.; Jones, D. E.; Kustin, Kenneth

doi:10.1021/ja01027a041

Cited by 65 publications

(30 citation statements)

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“…'v 1.6 (Sternlicht et al, 1968); log K3(30", p = 0.1) = 1.15 (O'Sullivan and Perrin, 1964). The corresponding enthalpies for KH and Kl are: AHH = 1.2 kcal/mol (Christensen and Izatt, 1962); AH1 = -3.0 kcal/mol (Martell and Taqui Khan, 1966 [ATPItotal ratios for these solutions, the broadening produced by them at 11.5 MHz is identical, within experimental error, at any temperature within the range studied.…”

Section: Treatment Of Data and Resultsmentioning

confidence: 99%

Measurement of the water exchange rate of bound water in the manganese(II)-adenosine triphosphate complex by oxygen-17 nuclear magnetic resonance

Zetter¹,

Dodgen²,

Hunt³

1973

Biochemistry

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Oxygen-1 7 line broadening measurements have been made on the MnATPz-complex in aqueous solution. The results are interpreted in terms of three kinetically equivalent waters being present in the inner sphere of the complex. The kinetic parameters for water exchange (per water molecule) are: k,,(25") = 5.0 x 107 sec-'; AH* = 9.6 kcal mol-'; AS* = 8.8 cal mol-! deg-1. These parameters are compared with published kinetic results for the substitution of 8-hydroxyquinoline into the inner sphere of MnATP2-and it is R ecent temperature-jump studies on the kinetics of manganese(I1) (Hague and Zetter, 1970; Hague et a/., 1972) and magnesium (Hague and Eigen, 1966; Hague et a / . , 1972) ternary complex formation and dissociation revealed several interesting results which may be significant in the understanding of Mg2+ and Mnz+ activation of enzymes. Of particular interest were the reactions of MnATP2-and MgATP2-with the anion of 8-hydroxyquinoline (Ox-), i.e.where M is Mg2+ or Mn2+. The rate of formation in this type of reaction is generally described (Hewkin and Prince, 1970) in terms of where KO, is a n outer sphere formation constant, dependent, in part, on the charge product of the reacting species, and k,, is the rate constant for the exchange of a solvent molecule between a metal ion (or complex) and the bulk solvent. For reaction 1, kf and the associated thermodynamic activation parameters for MgATP2-were consistent with eq 2 if it was assumed that k,, for MgATP2-was similar to that measured for Mg(H20)62+ (Neely and Connick, 1970). This was not the case for MnATP2-; kf was lower and the activation enthalpy higher than expected, suggesting that either k,, was lower than that measured for Mn(Hz0)62+ (Grant er al., 1971) or some other process-possibly a change in the type of coordination of the ATP to the Mn2T-was rate determining.The structure of the MnATP2-complex in aqueous solution has been the subject of much discussion. The picture that has emerged from numerous nmr studies indicates (1) that the a-, 8-, and y-phosphate groups (Cohn and Hughes, 1962; concluded that the generally considered mechanism for metal complex formation does not apply in this case. The discrepancy between these two sets of kinetic data is discussed in terms of possible binding differences of ATP in MnATP2-and 8-hydroxyquinoline-MnATP3-. It is suggested that these proposed differences can rationalize, in part, the similar behavior of Mn2+ and Mg2+ in the enzymatic activation of transphosphorylation reactions involving ATP.Sternlicht et al., 1965) and the adenine ring are bound to manganese, the latter being separated from the metal by an inner-sphere water molecule (Glassman er a/., 1971), and (2) that the complex contains three rapidly exchanging waters (Glassman et al., 1971).An I7O nmr study can further our knowledge of the properties of the MnATP2-complex in aqueous solution. Firstly, this method can sometimes give an indication of the number of water molecules in the complex. Secondly, it is sometimes possible to distinguish betw...

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Section: Treatment Of Data and Resultsmentioning

confidence: 99%

Measurement of the water exchange rate of bound water in the manganese(II)-adenosine triphosphate complex by oxygen-17 nuclear magnetic resonance

Zetter¹,

Dodgen²,

Hunt³

1973

Biochemistry

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“…Noat et al [16] considered the possible effects on the hexokinase reaction of the formation of the complex (ATP),Mg6- [24,25] and concluded that such complex formation was not significant. If such a complex were to form, but not to interact with the enzyme, apparent inhibition of NAD kinase would occur due to depletion of the substrate ATPMg2-; this would occur according to Equation (3), with K , = K , = 00 and K , = K , = K', the dissociation constant of the abortive complex :…”

Section: )mentioning

confidence: 99%

Kinetic Studies of the Interaction of Pigeon‐Liver NAD Kinase with Adenine Nucleotides and Divalent Cations

Apps¹,

Marsh²

1972

European Journal of Biochemistry

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1. NAD kinase is inhibited by free Mg2+, free ATP and by a number of other adenine nucleo-2. Inhibition by ATP, ADPMg-, ADP-ribose2-and AMP2-is competitive with respect to 3. ATP appears to bind equally well to the free enzyme and to binary enzyme substrate 4. The other adenine nucleotides studied have markedly less affinity for the free enzyme than 5. Mg2+ probably inhibits by forming a complex with NADt, which binds to the enzyme but 6. Low concentrations of Mg2+ reduce KgADf in an unexplained manner.7. ATPCa2-is a substrate for NAD kinase, but the rate-limiting step of the reaction may be tides.both ATPMg2-and NAD+.complexes.for binary complexes.is inactive in the reaction. different when other metals activate the enzyme.Although the ATP-dependent phosphotransferases have been widely studied in recent years, the role of divalent cations, which are obligatory cofactors for the reactions catalysed by these enzymes, is not completely understood. I n several instances [I -41 they are essential for the catalytic function of the enzyme but have little or no effect on the binding of adenine nucleotides, whereas in others [5] the metal ion may form a bridge between the protein and the nucleotide. Steady-state kinetic analysis can provide an indirect means of studying the interaction of such enzymes with the free nucleotide ATP4-or metal ion M2+, as well as the I : 1 complex, ATPM2-, which is the substrate of the reaction. I n the particular case of NAD kinase, previous studies [6-141 have usually been made with a small excess of divalent cation over ATP, so that the complex ATPM2-was the dominant species, with relatively low con- However, ATP afforded NAD kinase some protection from alkylation by bromoacetyl pyridine [17], and it was suggested that the free nucleotide might bind to the enzyme, perhaps a t a site separate from that occupied by ATPM2-. I n the present paper we report more detailed kinetic studies of the interaction of pigeon liver NAD kinase with ATP, Mg2+, Ca2+ and some other adenine nucleotides. MATERIALS AND METHODSReagents ATP (highest grade, from equine muscle), ADP and AMP were from Sigma. NAD+ was from Boehringer Mannheim GmbH (Mannheim, Germany). ADPribose was prepared by cleavage of NAD+ with Neurospora NAD glycohydrolase [ 181. Supplementary enzymes and their substrates were from Boehringer Mannheim GmbH (Mannheim, Germany).ATP, ADP and NAD+ were assayed as described previously [8] ; AMP and ADP-ribose were estimated by absorbance measurements at 260 nm. Ca2+, Co2+ and Mg2+ were used as their chlorides and Mn2+ and Zn2+ as their sulphates. CaCI, was standardized by titration against silver nitrate.

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“…The inconsistencies in the interpretation of the previous metal ion -ATP kinetic study by n.m.r. (39) have been pointed out in previous papers (17,35,40,41).…”

Section: Resultsmentioning

confidence: 83%

The Kinetics and Mechanisms of Exchange in the Binary System Manganese(II) – Adenosine 5′-Triphosphate

Kuntz¹,

Lam²,

Kotowycz³

1975

Can. J. Chem.

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. Can. J. Chem. 53,926 (1975). 31P n.m.r. studies on the Mn(I1) -adenosine 5'-triphosphate system indicate that two n.m.r. exchange mechanisms are present in solution; namely, the Eigen-Tamm mechanism and the direct ligand exchange mechanism. Their respective contributions to the observed n.m.r. linewidths and hence to the n.m.r. exchange rate depend upon the concentration of the ligand ATP. Equations are developed to prove what n.m.r. "sees" for the Eigen-Tamm mechanism and these equations are applied to this study. Chem. 53,926(1975). Des etudes r.m.n. de 3 1 P sur le systeme Mn(I1) -adenosine 5'-triphosphate indiquent que deux mecanismes d'echange en r.m.n. sont presents dans la solution, a savoir, le mkcanisme Eigen-Tamm et le mecanisme d'echange direct du ligand. Leurs contributions respectives a la largeur observee pour les bandes en r.m.n., ainsi qu'au taux d'echange en r.m.n., dependent de la concentration du ligand ATP. On a developpe des equations pour demontrer ce que la r.m.n. "voit" pour le mecanisme Eigen-Tamm et on a applique ces equations a I'etude actuelle.[Traduit par le journal] Introduction The application of nuclear magnetic resonance (n.m.r.) in the area of biochemistry is constantly increasing as n.m.r. determines not only whether two substances interact but also, in many cases, the sites of interaction. Excellent reviews in this area have been written by Roberts and Jardetzky (I), Rowe et al. (2), Mildvan and Cohn (3),

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Metal ion binding to adenosine triphosphate. III. Kinetic analysis

Cited by 65 publications

References 3 publications

Measurement of the water exchange rate of bound water in the manganese(II)-adenosine triphosphate complex by oxygen-17 nuclear magnetic resonance

Measurement of the water exchange rate of bound water in the manganese(II)-adenosine triphosphate complex by oxygen-17 nuclear magnetic resonance

Kinetic Studies of the Interaction of Pigeon‐Liver NAD Kinase with Adenine Nucleotides and Divalent Cations

The Kinetics and Mechanisms of Exchange in the Binary System Manganese(II) – Adenosine 5′-Triphosphate

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