Adenosine triphosphate, complexes with

Figure 13-2 (a) Structure of adenosine triphosphate (ATP), with ligand atoms shown in color. ib) Possible structure of a metal-ATP complex, with four bonds to ATP and two bonds to H2O ligands. 

Rechnitz, G.A. and Mohan, M.S., 1970, Potassium-adenosine triphosphate complex formation constant measured with ion-selective electrodes. Science 168 1460. 

ADP (adenosine diphosphate) and ATP (adenosine triphosphate) are complex organic molecules (Fig. 17.9) that, in essence, differ only hy the presence of an extra phosphate group in ATP. In the coupled reaction with glucose, about 38 mol of ATP are synthesized for every mole of glucose consumed. This gives an overall free energy change for the coupled reaction of... 

Figure 10-4. Adenosine triphosphate (ATP) shown as the magnesium complex. ADP forms a similar complex with Mg A...

Mg(II) forms a complex with adenosine triphosphate (ATP, 45), which at pH 7.2 and 37 °C has dissociation constant Kj = 3.8 x 10 molL-. The fraction of the total ATP which did not nndergo complexation present in a cell, (p, can be estimated on the basis of P NMR spectra by means of equation 5, where the snbscripts afi denote the chemical shift of P relative to that of P and the superscripts denote the valne measnred for... 

Chromium(III) forms stable complexes with adenosine-S -triphosphate.840,841,842 These are kinetically inert analogues of magnesium ATP complexes and may be used to study enzyme systems. The complexes prepared are chiral and may be distinguished in terms of chirality at the metal centre (198,199).843 The related complex of chromium(lll) with adenosine-5 -(l-thiodiphosphate) has been prepared the diastereoisomers were separated.844 The stereospecific synthesis of chromium(III) complexes of thiophosphates has been reported845 by the method outlined in equation (47), enabling the configuration of the thiophosphoryl centre to be determined. The availability of optically pure substrates will enable the stereospecificity of various enzyme systems to be investigated.845... 

A typical cross section of a cilium shows a ring formed by nine pairs of microtubules and two central tubules, i.e., the so-called nine + two pattern. Each doublet contains an A and a B subfibril with an inner and an outer dynein arm (a complex protein with ATPase activity) located on the A subfibril with radial spokes extending toward the central doublet. The ciliary membrane, which is an extension from the cell membrane of the epithelial cell, encloses the microtubules. The motion of the cilia is dependent on the sliding of the outer doublets past one another with the energy provided by adenosine triphosphate (ATP) through dynein ATPase activity. 

Figure 8.2.15 One-dimensional spectra acquired with the four-coil probe. Each sample (250 mM in D2O) was loaded into the coil via the attached Teflon tubes 32 scans were acquired for each spectrum, with no delay between excitations of successive coils. Concurrent with the switch position being incremented, the spectral width was optimized for each compound 1 Hz line-broadening was applied before Fourier transformation and baseline correction. The spectral widths were (a) 600 Hz (galactose) (b) 1400 Hz (adenosine triphosphate) (c) 2000 Hz (chloroquine) (d) 500 Hz (fructose). 2048 complex data points were acquired for each spectrum, giving data acquisition times of approximately 1.7, 0.7, 0.5 and 2.0 s, respectively. The delay between successive 90 degree excitations was 4.9 s for each sample. Reprinted with permission From Li, Y., Walters, A., Malaway, P., Sweedler, J. V. and Webb, A. G., Anal. Chem.,l, 4815-4820 (1999). Copyright (1999) American Chemical Society...

Precipitation of the cytoplasm by the formation of complexes with phosphated entities, such as adenosine triphosphate and nucleic acids... 

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