A Raman study of the binding of Fe(III) to ATP and AMP

Abstract

ATP-Fe and AMP-Fe complexes in water (H2O and 2H2O) at pH 7.5 were studied using Raman spectroscopy. Parallel and perpendicular polarization spectra were recorded in the spectral range 200-1650 cm-1, and the depolarization ratios for most of the bands were calculated. The changes in the frequencies, intensities and depolarization ratios of the ATP and AMP bands after the addition of FeCl3 showed that the adenine moiety, in addition to the phosphate(s), was involved in the binding of Fe to both ATP and AMP. Direct interactions of Fe(III) with the phosphate chain and the N-7 nitrogen and indirect interaction (via water molecules) with the amide group were proposed for the ATP-Fe complex. In contrast, direct interaction with the phosphate group and indirect interaction with the amide group were observed for the AMP-Fe complex. The different interactions of the two complexes suggest an 'anti' conformation for the ATP-Fe complex and a 'syn' conformation for the AMP-Fe complex. The strong binding of Fe to ATP compared with AMP and the difference in the conformation of the ATP-Fe and the AMP-Fe complexes may be significant in the pathway of Fe release in mitochondria.

Characterization of the binding of Fe(III) to F1ATPase from bovine heart mitochondria

“…Specifically, Mg(II) and other divalent cations interact strongly with the phosphate moiety and indirectly with the adenine moiety [26]. In contrast, Fe(III) is directly coordinated both to the phosphate chain and the N-7 ring position of adenine [23].…”

Effects of changes in intracellular iron pool on AlkB-dependent and AlkB-independent mechanisms protecting E.coli cells against mutagenic action of alkylating agent

“…More efficient than dATP self-dealkylation of dCTP most probably results from the favorable location of an etheno adduct within 3.5 Å of the iron. This mechanism is strongly supported by Raman spectroscopy [52], and 1 H and 31 P NMR relaxation study [53,54].…”

Nano‐bio interface study between Fe content TiO2 nanoparticles and adenosine triphosphate biomolecules

“…The ribose moiety has weak Raman scattering in than have other moieties in pure ATP spectrum, which gets enhanced, showing a sharp peak at 553.20 cm −1 on hydrolysis due the perturbation of other vibration modes associated with it. The sharp peaks at 699 cm −1 represent the out‐of‐plane waging of NH 2 bonds and at 721.1 cm −1 resemblance the adenine ring breathing mode, when all the bonds stretch coherently or might arise because of the vibrations from adenine perturbed ribose rings as D.N 9 R and N 1 C 4 bonds, where R represents the ribose rings . Hydrolysis causes structural deformation mostly affecting the adenine ring modes.…”

“…Vibrational spectra can give broad knowledge with respect to the molecular conformation and can be obtained by Raman spectroscopy. The Raman studies of the binding of divalent metal ions with the triphosphate moiety of ATP were reported by Rimai et al Zhelyaskov and Yue have shown that iron(III) has the ability to bind to ATP and adenosine monophosphate (AMP) by studying Raman spectral lines . Bhaumik et al also reported the interaction study of ZnO with ATP biomolecules by using Raman spectroscopy .…”