Electron transfer between guanosine radicals and amino acids in aqueous solution. II. Reduction of guanosine radicals by tryptophan

Article Abstract:

The efficiency of the chemical pathway of DNA repair is analyzed by using time-resolved chemically induced dynamic nuclear polarization (CIDNP) using the model system having guanosyl base radicals and tryptophan as the electron donor. The rate constants of electron transfer from the amino acid to the guanosyl radical is higher than the corresponding values for electron transfer in the case of N-acetyl tyrosine as the reducing agent.

Biological Product (except Diagnostic) Manufacturing, Drugs, Guanine, DNA repair, Optical properties, Structure, Polarization (Light)

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Reversibility of electron transfer in tryptophan-tyrosine peptide in acidic aqueous solution studied by time-resolved CIDNP

Article Abstract:

A study was conducted on electron transfer reactions in tryptophan-tyrosine peptide under strongly acidic conditions using time-resolved chemically induced dynamic nuclear polarization (CIDNP). Analysis of the CIDNP kinetics revealed that the rate constant of the reaction k(sub f) stays unchanged upon pH variation, whereas the rate constant of electron transfer in the opposite direction K(sub r) increases with decreasing pH.

Peptides

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Intramolecular electron transfer in tryptophan-tyrosine peptide in photoinduced reaction in aqueous solution

Article Abstract:

The photochemical reactions are studied in its triplet state with the tryptophan-tyrosine dipeptide with 1:1 mixture of N-acetyl tryptophan and N-acetyl tyrosine in acid, neutral and base solutions. The study reveals the strong effect of linkage on the amplitude and kinetics of spin polarization, and helps to study the structure and folding kinetics of proteins.

Molecules, Aqueous solution reactions, Atomic properties

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