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The reaction of superoxide, formate radical, and hydrated electron with transferrin and its model compound, Fe(III)-ethylenediamine-N,N'-bis[2-(2-hydroxyphenyl)acetic acid] as studied by pulse radiolysis
Journal article   Open access   Peer reviewed

The reaction of superoxide, formate radical, and hydrated electron with transferrin and its model compound, Fe(III)-ethylenediamine-N,N'-bis[2-(2-hydroxyphenyl)acetic acid] as studied by pulse radiolysis

Garry R Buettner
The Journal of biological chemistry, Vol.262(25), pp.11995-11998
1987
DOI: 10.1016/S0021-9258(18)45308-2
PMID: 3040725
url
https://doi.org/10.1016/S0021-9258(18)45308-2View
Published (Version of record) Open Access

Abstract

Transferrin and the transferrin model compound Fe(III)-EHPG (Fe(III)-ethylenediamine-N,N'-bis[2-(2-hydroxyphenyl)acetic acid] were found not to react with superoxide, as pulse radiolysis and kinetic spectroscopy revealed no transient species and no bleaching of the 465-nm absorption. However, transferrin was found to react with the formate radical, CO-.2, and the hydrated electron, e-aq, with second-order rate constants of 3.8 × 10(8) and 1.1 × 10(10) M-1 S-1, respectively. These reactions produced a transient species (lambda max = 420 nm) which subsequently decayed by a second-order process. However, no reduction of the Fe(III) in transferrin was detected. Fe(III)-EHPG was also found to react with CO-.2 and e-aq, k = 7.3 × 10(6) and 1.1 × 10(9) M-1 S-1, respectively. The reactions of CO-.2 and e-aq with Fe(III)-EHPG resulted in no transient species but rather in reduction of the iron. These results are consistent with the inability of transferrin and Fe(III)-EHPG to catalyze the Haber-Weiss reaction.
Fundamental and applied biological sciences. Psychology Proteins Biological and medical sciences Analytical, structural and metabolic biochemistry Metalloproteins Other metalloproteins

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