THE MECHANISM OF THE RADIATION-INDUCED OXIDATION AND REDUCTION OF INORGANIC ACCEPTORS IN ACETONE SOLUTION

Journal Article · Sun Apr 21 04:00:00 EST 1963 · Doklady Akademii Nauk SSSR (U.S.S.R.) English translation currently published in a number of subject-oriented journals

OSTI ID:4686023

Bakh, N A; Roder, M; Bugaenko, L T

The results of studies on the electron paramagnetic resonance (EPR) spectrum of irradiated proteins show that an unpaired electron is localized in some sort of trap in the irradiated protein molecule (super-fine splitting of the EPR signal), and that the multiplet form of the spectrum is due to the presence of cystine and cysteine in the irradiated molecule. If the electron could be liberated from the trap, the form of the EPR signal shouid become that of a singlet, and the intensity of the signal should decrease. To test this hypothesis, dried protein samples of pepsin, serum and egg albumin, dried rabbit muscle tissue, and denatured pepsin were subjected to a gamma radiation dose of 5 to 10 million r at room temperature in a vacuum of about 10/sup -3/ mm Hg std. The irradiated samples at room temperature gave a doublet EPR signal on a background of a cysteine'' multiplet structure. The shape of the spectrum did not change on cooling the irradiated samples to -- 196 deg C. On irradiating the irradiated samples with the light from a mercury vapor lamp in the region of 365 to 750 mu , no change in the EPR spectrum could be detected. On irradiating the irradiated protein samples with infrared light from a muffle furnace with a wavelength of 3.5 mu (energy of 0.34 ev) for 2 to 3 hours, the EPR doublet signal at liquid nitrogen temperatures was converted to a singlet having a total width less than the total width of the doublet. The cysteine'' background signal did not change. The pepsin denatured by boiling maintained the doublet form of the EPR spectrum. The infrared irradiation mobilized the trapped electron, and converted the free radical formed by irradiation to a chemically active form which could react with the surrounding molecules. (TTT)

• Research Organization: Moscow State Univ.; Inst. of Electrochemistry, Academy of Sciences, USSR
• NSA Number: NSA-17-028958
• OSTI ID: 4686023
• Journal Information: Doklady Akademii Nauk SSSR (U.S.S.R.) English translation currently published in a number of subject-oriented journals, Journal Name: Doklady Akademii Nauk SSSR (U.S.S.R.) English translation currently published in a number of subject-oriented journals Vol. Vol: 149; ISSN DANKA
• Country of Publication: Country unknown/Code not available
• Language: Russian

Related Subjects

ACCEPTORS
CHEMICAL REACTIONS
CHEMISTRY
CHROMIUM COMPOUNDS
COPPER COMPOUNDS
DECOMPOSITION
ELECTRONS
IODINE
IRON COMPOUNDS
IRRADIATION
MANGANESE COMPOUNDS
NITROGEN
ORGANIC ACIDS
OXIDATION
POTASSIUM IODIDES
PRESSURE
RADIATION CHEMISTRY
RADIATION EFFECTS
RADIOLYSIS
SEALS
SOLUTIONS
TUBES
VACUUM
X RADIATION