Reduction of ferrylmyoglobin by cysteine as affected by pH

S.H. Libardi; Helene Pindstrup Kristensen; Jose Manuel Amigo Rubio; D.R. Cardoso; Leif Horsfelt Skibsted

doi:10.1039/c4ra10562a

Reduction of ferrylmyoglobin by cysteine as affected by pH

S.H. Libardi, Helene Pindstrup Kristensen, Jose Manuel Amigo Rubio, D.R. Cardoso, Leif Horsfelt Skibsted

7 Citationer (Scopus)

Abstract

Reduction of the hypervalent meat pigment ferrylmyoglobin, MbFe(iv)O, by cysteine is enhanced by acid due to protonation of ferrylmyoglobin to yield sulfmyoglobin as the main product, while at alkaline conditions, the rate decreases with the cysteine dianion as the reactant forming oxymyoglobin, MbFe(ii)O₂. The second-order rate constant for cysteine reacting with protonated ferrylmyoglobin is 5.1 ± 0.4 L mol^-1 s^-1 at 25 °C in 0.16 M aqueous sodium chloride and for the cysteine dianion reacting with ferrylmyoglobin 0.31 ± 0.15 L mol^-1 s^-1. For pH = 7.4 the activation parameters for sulfmyoglobin formation is ΔH^‡ = 75 ± 2 kJ mol^-1 and ΔS^‡ = -250 ± 7 J mol^-1 K^-1 with similar values for homocysteine and glutathione. The difference in product is indicative of a shift from an electron-transfer/radical addition mechanism at low pH as in the stomach to a two-step electron-transfer mechanism at higher pH as in the intestine, and is discussed in relation to protection against the formation of radicals by sulphurous compounds during the digestion of red meat.

Originalsprog	Engelsk
Tidsskrift	R S C Advances
Vol/bind	4
Udgave nummer	105
Sider (fra-til)	60953-60958
Antal sider	6
ISSN	2046-2069
DOI	https://doi.org/10.1039/c4ra10562a
Status	Udgivet - 2014

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10.1039/c4ra10562a

Citationsformater

@article{2df424854fb24a648c1821ed923445ff,

title = "Reduction of ferrylmyoglobin by cysteine as affected by pH",

abstract = "Reduction of the hypervalent meat pigment ferrylmyoglobin, MbFe(iv)O, by cysteine is enhanced by acid due to protonation of ferrylmyoglobin to yield sulfmyoglobin as the main product, while at alkaline conditions, the rate decreases with the cysteine dianion as the reactant forming oxymyoglobin, MbFe(ii)O2. The second-order rate constant for cysteine reacting with protonated ferrylmyoglobin is 5.1 ± 0.4 L mol-1 s-1 at 25 °C in 0.16 M aqueous sodium chloride and for the cysteine dianion reacting with ferrylmyoglobin 0.31 ± 0.15 L mol-1 s-1. For pH = 7.4 the activation parameters for sulfmyoglobin formation is ΔH‡ = 75 ± 2 kJ mol-1 and ΔS‡ = -250 ± 7 J mol-1 K-1 with similar values for homocysteine and glutathione. The difference in product is indicative of a shift from an electron-transfer/radical addition mechanism at low pH as in the stomach to a two-step electron-transfer mechanism at higher pH as in the intestine, and is discussed in relation to protection against the formation of radicals by sulphurous compounds during the digestion of red meat.",

author = "S.H. Libardi and Kristensen, {Helene Pindstrup} and {Amigo Rubio}, {Jose Manuel} and D.R. Cardoso and Skibsted, {Leif Horsfelt}",

year = "2014",

doi = "10.1039/c4ra10562a",

language = "English",

volume = "4",

pages = "60953--60958",

journal = "RSC Advances",

issn = "2046-2069",

publisher = "RSC Publishing",

number = "105",

}

TY - JOUR

T1 - Reduction of ferrylmyoglobin by cysteine as affected by pH

AU - Libardi, S.H.

AU - Kristensen, Helene Pindstrup

AU - Amigo Rubio, Jose Manuel

AU - Cardoso, D.R.

AU - Skibsted, Leif Horsfelt

PY - 2014

Y1 - 2014

N2 - Reduction of the hypervalent meat pigment ferrylmyoglobin, MbFe(iv)O, by cysteine is enhanced by acid due to protonation of ferrylmyoglobin to yield sulfmyoglobin as the main product, while at alkaline conditions, the rate decreases with the cysteine dianion as the reactant forming oxymyoglobin, MbFe(ii)O2. The second-order rate constant for cysteine reacting with protonated ferrylmyoglobin is 5.1 ± 0.4 L mol-1 s-1 at 25 °C in 0.16 M aqueous sodium chloride and for the cysteine dianion reacting with ferrylmyoglobin 0.31 ± 0.15 L mol-1 s-1. For pH = 7.4 the activation parameters for sulfmyoglobin formation is ΔH‡ = 75 ± 2 kJ mol-1 and ΔS‡ = -250 ± 7 J mol-1 K-1 with similar values for homocysteine and glutathione. The difference in product is indicative of a shift from an electron-transfer/radical addition mechanism at low pH as in the stomach to a two-step electron-transfer mechanism at higher pH as in the intestine, and is discussed in relation to protection against the formation of radicals by sulphurous compounds during the digestion of red meat.

AB - Reduction of the hypervalent meat pigment ferrylmyoglobin, MbFe(iv)O, by cysteine is enhanced by acid due to protonation of ferrylmyoglobin to yield sulfmyoglobin as the main product, while at alkaline conditions, the rate decreases with the cysteine dianion as the reactant forming oxymyoglobin, MbFe(ii)O2. The second-order rate constant for cysteine reacting with protonated ferrylmyoglobin is 5.1 ± 0.4 L mol-1 s-1 at 25 °C in 0.16 M aqueous sodium chloride and for the cysteine dianion reacting with ferrylmyoglobin 0.31 ± 0.15 L mol-1 s-1. For pH = 7.4 the activation parameters for sulfmyoglobin formation is ΔH‡ = 75 ± 2 kJ mol-1 and ΔS‡ = -250 ± 7 J mol-1 K-1 with similar values for homocysteine and glutathione. The difference in product is indicative of a shift from an electron-transfer/radical addition mechanism at low pH as in the stomach to a two-step electron-transfer mechanism at higher pH as in the intestine, and is discussed in relation to protection against the formation of radicals by sulphurous compounds during the digestion of red meat.

U2 - 10.1039/c4ra10562a

DO - 10.1039/c4ra10562a

M3 - Journal article

SN - 2046-2069

VL - 4

SP - 60953

EP - 60958

JO - RSC Advances

JF - RSC Advances

IS - 105

ER -

Reduction of ferrylmyoglobin by cysteine as affected by pH

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