Oxidation of carbon monoxide by perferrylmyoglobin
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Oxidation of carbon monoxide by perferrylmyoglobin. / Libardi, Silvia H; Skibsted, Leif Horsfelt; Cardoso, Daniel R.
I: Journal of Agricultural and Food Chemistry, Bind 62, Nr. 8, 2014, s. 1950-1955.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Oxidation of carbon monoxide by perferrylmyoglobin
AU - Libardi, Silvia H
AU - Skibsted, Leif Horsfelt
AU - Cardoso, Daniel R
PY - 2014
Y1 - 2014
N2 - Perferrylmyoglobin is found to oxidize CO in aerobic aqueous solution to CO2. Tryptophan hydroperoxide in the presence of tetra(4-sulfonatophenyl)-porphyrinate-iron(III) or simple iron(II)/(III) salts shows similar reactivity against CO. The oxidation of CO is for tryptophan hydroperoxide concluded to depend on the formation of alkoxyl radicals by reductive cleavage by iron(II) or on the formation of peroxyl radicals by oxidative cleavage by iron(III). During oxidation of CO, the tryptophan peroxyl radical was depleted with a rate constant of 0.26 ± 0.01 s(-1) for CO-saturated aqueous solution of pH 7.4 at 25 °C without concomitant reduction of the iron(IV) center. Carbon monoxide is as a natural metabolite accordingly capable of scavenging tryptophan radicals in myoglobin activated by peroxides with a second-order rate constant of (3.3 ± 0.6) × 10(2) L mol(-1) s(-1), a reaction that might be of importance in cellular membranes of the intestine for protection of tissue against radical damage during meat digestion.
AB - Perferrylmyoglobin is found to oxidize CO in aerobic aqueous solution to CO2. Tryptophan hydroperoxide in the presence of tetra(4-sulfonatophenyl)-porphyrinate-iron(III) or simple iron(II)/(III) salts shows similar reactivity against CO. The oxidation of CO is for tryptophan hydroperoxide concluded to depend on the formation of alkoxyl radicals by reductive cleavage by iron(II) or on the formation of peroxyl radicals by oxidative cleavage by iron(III). During oxidation of CO, the tryptophan peroxyl radical was depleted with a rate constant of 0.26 ± 0.01 s(-1) for CO-saturated aqueous solution of pH 7.4 at 25 °C without concomitant reduction of the iron(IV) center. Carbon monoxide is as a natural metabolite accordingly capable of scavenging tryptophan radicals in myoglobin activated by peroxides with a second-order rate constant of (3.3 ± 0.6) × 10(2) L mol(-1) s(-1), a reaction that might be of importance in cellular membranes of the intestine for protection of tissue against radical damage during meat digestion.
U2 - 10.1021/jf4053176
DO - 10.1021/jf4053176
M3 - Journal article
C2 - 24506496
VL - 62
SP - 1950
EP - 1955
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
SN - 0021-8561
IS - 8
ER -
ID: 101955229