Proton transfer reactions of nucleic acid bases: A semiempirical molecular orbital study

Venkateswarlu, Divi; Lyngdoh, R. H. Duncan

doi:10.1007/bf02884440

Cited by 3 publications

(1 citation statement)

References 42 publications

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“…Experiments, under conditions where H/D KIE were measured, gave k (H 2 O)/ k (D 2 O) = 2.4 ± 0.4 at pH = 6.0 with MS-EPT dominating and at pH = 8 with k (H 2 O)/ k (D 2 O) = 1.3 ± 0.2 with PT–ET dominating. The values are relatively small but consistent with H/D isotope effects observed in other PCET reactions. − For example, transient absorption measurements on GMPH oxidation by purine radicals show that the reactions occur with KIE of 1.5–2. ,, The small KIE for PT suggest that the extent of PT in both reactions is relatively small compared to the overall distance for PT in both PT reactions. − …”

Section: Discussionsupporting

confidence: 71%

Proton-Coupled Electron Transfer in the Oxidation of Guanosine Monophosphate by Ru(bpy)₃³⁺

et al. 2018

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Oxidation of guanine by the outer-sphere metal complex oxidant Ru(bpy)3 3+ (bpy is 2,2′-bipyridine) has been explored in deoxyguanosine-5′-monophosphate with the added buffers succinic acid/succinate Hsuc/suc–• (pK a = 5.6), H2PO4 –/HPO4 2– (pK a = 7.2), and Tris [(HOCH2)3CNH3 +/(HOCH2)3CNH2] (pK a = 8.1) at 23 ± 2 °C. Over an extended range of buffer concentrations and ratios, there is clear evidence for the mechanistic importance of pathways involving concerted electron–proton transfer. In this pathway, proton transfer to the base form of the buffer occurs in concert with electron transfer to the oxidant, Ru(bpy)3 3+.

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Section: Discussionsupporting

confidence: 71%

Proton-Coupled Electron Transfer in the Oxidation of Guanosine Monophosphate by Ru(bpy)₃³⁺

et al. 2018

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Magnetooptic rotation and molecular polarizability of PEG

Murthy¹,

Naidu²

1978

Journal of Quantitative Spectroscopy and Radiative Transfer

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Structure-wise discrimination of cytosine, thymine, and uracil by proteins in terms of their nonbonded interactions

Usha

Selvaraj

2013

Journal of Biomolecular Structure and Dynamics

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The molecular recognition and discrimination of very similar ligand moieties by proteins are important subjects in protein-ligand interaction studies. Specificity in the recognition of molecules is determined by the arrangement of protein and ligand atoms in space. The three pyrimidine bases, viz. cytosine, thymine, and uracil, are structurally similar, but the proteins that bind to them are able to discriminate them and form interactions. Since nonbonded interactions are responsible for molecular recognition processes in biological systems, our work attempts to understand some of the underlying principles of such recognition of pyrimidine molecular structures by proteins. The preferences of the amino acid residues to contact the pyrimidine bases in terms of nonbonded interactions; amino acid residue-ligand atom preferences; main chain and side chain atom contributions of amino acid residues; and solvent-accessible surface area of ligand atoms when forming complexes are analyzed. Our analysis shows that the amino acid residues, tyrosine and phenyl alanine, are highly involved in the pyrimidine interactions. Arginine prefers contacts with the cytosine base. The similarities and differences that exist between the interactions of the amino acid residues with each of the three pyrimidine base atoms in our analysis provide insights that can be exploited in designing specific inhibitors competitive to the ligands.

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Proton transfer reactions of nucleic acid bases: A semiempirical molecular orbital study

Cited by 3 publications

References 42 publications

Proton-Coupled Electron Transfer in the Oxidation of Guanosine Monophosphate by Ru(bpy)₃³⁺

Proton-Coupled Electron Transfer in the Oxidation of Guanosine Monophosphate by Ru(bpy)₃³⁺

Magnetooptic rotation and molecular polarizability of PEG

Structure-wise discrimination of cytosine, thymine, and uracil by proteins in terms of their nonbonded interactions

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Proton transfer reactions of nucleic acid bases: A semiempirical molecular orbital study

Cited by 3 publications

References 42 publications

Proton-Coupled Electron Transfer in the Oxidation of Guanosine Monophosphate by Ru(bpy)33+

Proton-Coupled Electron Transfer in the Oxidation of Guanosine Monophosphate by Ru(bpy)33+

Magnetooptic rotation and molecular polarizability of PEG

Structure-wise discrimination of cytosine, thymine, and uracil by proteins in terms of their nonbonded interactions

Contact Info

Product

Resources

About

Proton-Coupled Electron Transfer in the Oxidation of Guanosine Monophosphate by Ru(bpy)₃³⁺

Proton-Coupled Electron Transfer in the Oxidation of Guanosine Monophosphate by Ru(bpy)₃³⁺