Proton-coupled electron transfer promotes the reduction of ferrylmyoglobin by uric acid under physiological conditions
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Proton-coupled electron transfer promotes the reduction of ferrylmyoglobin by uric acid under physiological conditions. / Zawadzki, Andressa; Cardoso, Daniel R.; Skibsted, Leif Horsfelt.
In: RSC Advances, Vol. 29, No. 7, 2017, p. 17824-17831.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Proton-coupled electron transfer promotes the reduction of ferrylmyoglobin by uric acid under physiological conditions
AU - Zawadzki, Andressa
AU - Cardoso, Daniel R.
AU - Skibsted, Leif Horsfelt
PY - 2017
Y1 - 2017
N2 - The hypervalent muscle pigment ferrylmyoglobin, MbFe(IV)]O, is not reduced by urate monoanions at physiological conditions despite a strong driving force of around 30 kJ mol1 while for low pH, uric acid was found to reduce protonated ferrylmyoglobin, MbFe(IV)]O,H+, efficiently in a bimolecular reaction with k1 ¼ 1.1 0.1 103 L mol1 s1, DH‡ ¼ 66.1 0.1 kJ mol1 and DS‡ ¼ 35.2 0.2 J mol1K1. For intermediate pH, like for anaerobic muscles and for meat, proton-oupled electron transfer occurs in a transition state, {MbFe(IV)]O/H+/urate}‡, which is concluded to be formed from uric acid and MbFe(IV)]O rather than from urate and MbFe(IV)]O,H+ with k3 ¼ 9.7 0.6 102 L mol1 s1, DH‡ ¼ 59.2 0.1 kJ mol1 and DS‡ ¼ 11.5 0.3 J mol1 K1. The activation parameters as calculated fromthe temperature dependence of the pH-reduction profile in aqueous 0.067 mol L1 NaCl (from 25 C up to 40 C), support a mechanism for reduction of hypervalent heme iron, where initial proton transfer to oxo-iron initiates the intermolecular electron transfer from urate to ferrylmyoglobin. The concentrationof the powerful prooxidant ferrylmyoglobin increases strongly during digestion of red meat in the stomach. A concomitant increase in uric acid concentration may serve as an inherent protection against radical formation by ferrylmyoglobin
AB - The hypervalent muscle pigment ferrylmyoglobin, MbFe(IV)]O, is not reduced by urate monoanions at physiological conditions despite a strong driving force of around 30 kJ mol1 while for low pH, uric acid was found to reduce protonated ferrylmyoglobin, MbFe(IV)]O,H+, efficiently in a bimolecular reaction with k1 ¼ 1.1 0.1 103 L mol1 s1, DH‡ ¼ 66.1 0.1 kJ mol1 and DS‡ ¼ 35.2 0.2 J mol1K1. For intermediate pH, like for anaerobic muscles and for meat, proton-oupled electron transfer occurs in a transition state, {MbFe(IV)]O/H+/urate}‡, which is concluded to be formed from uric acid and MbFe(IV)]O rather than from urate and MbFe(IV)]O,H+ with k3 ¼ 9.7 0.6 102 L mol1 s1, DH‡ ¼ 59.2 0.1 kJ mol1 and DS‡ ¼ 11.5 0.3 J mol1 K1. The activation parameters as calculated fromthe temperature dependence of the pH-reduction profile in aqueous 0.067 mol L1 NaCl (from 25 C up to 40 C), support a mechanism for reduction of hypervalent heme iron, where initial proton transfer to oxo-iron initiates the intermolecular electron transfer from urate to ferrylmyoglobin. The concentrationof the powerful prooxidant ferrylmyoglobin increases strongly during digestion of red meat in the stomach. A concomitant increase in uric acid concentration may serve as an inherent protection against radical formation by ferrylmyoglobin
U2 - 10.1039/c6ra28314d
DO - 10.1039/c6ra28314d
M3 - Journal article
VL - 29
SP - 17824
EP - 17831
JO - RSC Advances
JF - RSC Advances
SN - 2046-2069
IS - 7
ER -
ID: 174594826