Mechanism of oxidation of cysteine and methionine by ferrate(VI): Mössbauer investigation
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Oxidation of organosulfur compounds (S) by ferrate(VI) (FeVIO42-,Fe(VI)) proceeds by the transfer of oxygen atom to S. A vast amount of literature proposed oxygen atom transfer (OAT) via 2-e-transfer process in which Fe(IV) acts as an intermediate, and Fe(II) was also proposed to be an intermediate or final reduced iron species of Fe(VI)(FeVI→FeIV→FeII). In this paper, Mössbauer spectroscopy was applied to explore intermediate iron species in the oxidation of cysteine (Cys) and methionine (Met) by Fe(VI). In the oxidation of Cys, both Fe(II) and Fe(III) were observed while only Fe(III) was seen in the oxidation of Met by Fe(VI). These results support that no Fe(II) species was formed in the oxidation of Met before forming Fe(III). These results are in consistency with the possibility of initial 1-e-transfer with the formation of Fe(V) species and subsequent 2-e-transfer to yield Fe(III)(FeVI→ FeV→FeIII). © 2012 American Institute of Physics.
author list (cited authors)
Sharma, V. K., Siskova, K., Machala, L., & Zboril, R.