Reduction of ferricytochrome c, methemoglobin and metmyoglobin by hydroxyl and alcohol radicals

Leeuwen, Johan W. van; Tromp, Jan; Nauta, H.

doi:10.1016/0005-2795(79)90043-6

Cited by 24 publications

(3 citation statements)

References 19 publications

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“…The reactions of cytochrome c with various radicals generated by pulse radiolysis has been reviewed [17]. Briefly, hydroxyl and hydrogen radicals react with iron(II) cytochrome c and iron(III) cytochrome c at diffusion-controlled rates to ultimately produce, respectively, partially iron(III) cytochrome c and iron(II) cytochrome c; the primary targets are amino acid residues, which then undergo redox reactions with the haem [18][19][20][21][22]. Br 2…”

Section: •-mentioning

confidence: 99%

“…In the presence of iron(II) cytochrome c or iron(III) cytochrome c, reactions of hydroxyl and hydrogen radicals with the protein compete with the reactions in Eqs. 2, 3, 4, 5 and 6: hydroxyl and hydrogen radicals react with iron(III) cytochrome c with rate constants of 1.4 • 10 10 M -1 s -1 [22] and 1.1 • 10 10 M -1 s -1 [18,19], respectively, to give, among other products, 25-55% iron(II) cytochrome c [21] and 50% iron(II) cytochrome c [18,19], respectively. The corresponding rate constants for the reactions of these radicals with iron(II) cytochrome c are higher than 1 • 10 10 M -1 s -1 [20] and 1.3 • 10 10 M -1 s -1 , respectively [19].…”

Section: Generation Of Co 3 •By Pulse Radiolysis In the Presence Of Cytochrome Cmentioning

confidence: 99%

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Oxidation-state-dependent reactions of cytochrome c with the trioxidocarbonate(•1−) radical: a pulse radiolysis study

Domazou

Koppenol

2006

J Biol Inorg Chem

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The reaction of the trioxidocarbonate(*1-) radical (CO (3) (*-) , "carbonate radical anion") with cytochrome c was studied by pulse radiolysis at alkaline pH and room temperature. With iron(III) cytochrome c, CO (3) (*-) reacts with the protein moiety with rate constants of (5.1 +/- 0.6) x 10(7) M(-1) s(-1) (pH 8.4, I approximately 0.27 M) and (1.0 +/- 0.2) x 10(8) M(-1) s(-1) (pH 10, I = 0.5 M). The absorption spectrum of the haem moiety was not changed, thus, amino acid radicals produced on the protein do not reduce the haem. The pH-dependent difference in rate constants may be attributed to differences in ionization states of amino acids and to the change in the conformation of the protein. With iron(II) cytochrome c, CO (3) (*-) oxidizes the haem quantitatively, presumably via electrostatic guidance of the radical to the solvent-accessible haem edge, with a different pH dependence: at pH 8.4, the rate constant is (1.1 +/- 0.1) x 10(9) M(-1) s(-1) and, at pH 10, (7.6 +/- 0.6) x 10(8) M(-1) s(-1). We propose that CO (3) (*-) oxidizes the iron center directly, and that the lower rate observed at pH 10 is due to the different charge distribution of iron(II) cytochrome c.

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Section: •-mentioning

confidence: 99%

Section: Generation Of Co 3 •By Pulse Radiolysis In the Presence Of Cytochrome Cmentioning

confidence: 99%

Oxidation-state-dependent reactions of cytochrome c with the trioxidocarbonate(•1−) radical: a pulse radiolysis study

Domazou

Koppenol

2006

J Biol Inorg Chem

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“…reducing properties (E°' = -0.97 V) (81). On the other hand, the Compound II-like species might oxidize to a Compound I via a one-electron redox coupling with the microsomal non-heme iron (45).…”

Section: Factors Promoting the Release Of Fe(ii) From Ferritinmentioning

confidence: 99%

Sources and role of iron in lipid peroxidation

Minotti¹

1993

Chem. Res. Toxicol.

144

102

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Pulse Radiolysis and Ultra‐High‐Performance Liquid Chromatography/High‐Resolution Mass Spectrometry Studies on the Reactions of the Carbonate Radical with Vitamin B₁₂ Derivatives

Dassanayake

Shelley

Cabelli

et al. 2015

Chemistry A European J

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The reactions of the carbonate radical anion (CO3 (.) (-) ) with vitamin B12 derivatives were studied by pulse radiolysis. The carbonate radical anion directly oxidizes the metal center of cob(II)alamin quantitively to give hydroxycobalamin, with a bimolecular rate constant of 2.0×10(9) M(-1) s(-1) . The reaction of CO3 (.) (-) with hydroxycobalamin proceeds in two steps. The second-order rate constant for the first reaction is 4.3×10(8) M(-1) s(-1) . The rate of the second reaction is independent of the hydroxycobalamin concentration and is approximately 3.0×10(3) s(-1) . Evidence for formation of corrinoid complexes differing from cobalamin by the abstraction of two or four hydrogen atoms from the corrin macrocycle and lactone ring formation has been obtained by ultra-high-performance liquid chromatography/high-resolution mass spectrometry (UHPLC/HRMS). A mechanism is proposed in which abstraction of a hydrogen atom by CO3 (.) (-) from a carbon atom not involved in the π conjugation system of the corrin occurs in the first step, resulting in formation of a Co(III) C-centered radical that undergoes rapid intramolecular electron transfer to form the corresponding Co(II) carbocation complex for about 50 % of these complexes. Subsequent competing pathways lead to formation of corrinoid complexes with two fewer hydrogen atoms and lactone derivatives of B12 . Our results demonstrate the potential of UHPLC combined with HRMS in the separation and identification of tetrapyrrole macrocycles with minor modifications from their parent molecule.

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Reduction of ferricytochrome c, methemoglobin and metmyoglobin by hydroxyl and alcohol radicals

Cited by 24 publications

References 19 publications

Oxidation-state-dependent reactions of cytochrome c with the trioxidocarbonate(•1−) radical: a pulse radiolysis study

Oxidation-state-dependent reactions of cytochrome c with the trioxidocarbonate(•1−) radical: a pulse radiolysis study

Sources and role of iron in lipid peroxidation

Pulse Radiolysis and Ultra‐High‐Performance Liquid Chromatography/High‐Resolution Mass Spectrometry Studies on the Reactions of the Carbonate Radical with Vitamin B₁₂ Derivatives

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Reduction of ferricytochrome c, methemoglobin and metmyoglobin by hydroxyl and alcohol radicals

Cited by 24 publications

References 19 publications

Oxidation-state-dependent reactions of cytochrome c with the trioxidocarbonate(•1−) radical: a pulse radiolysis study

Oxidation-state-dependent reactions of cytochrome c with the trioxidocarbonate(•1−) radical: a pulse radiolysis study

Sources and role of iron in lipid peroxidation

Pulse Radiolysis and Ultra‐High‐Performance Liquid Chromatography/High‐Resolution Mass Spectrometry Studies on the Reactions of the Carbonate Radical with Vitamin B12 Derivatives

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Product

Resources

About

Pulse Radiolysis and Ultra‐High‐Performance Liquid Chromatography/High‐Resolution Mass Spectrometry Studies on the Reactions of the Carbonate Radical with Vitamin B₁₂ Derivatives