Reaction of ferric leghemoglobin with H2O2: formation of heme-protein cross-links and dimeric species

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Reaction of ferric leghemoglobin with H2O2 : formation of heme-protein cross-links and dimeric species. / Moreau, S; Davies, M J; Puppo, A.

In: Biochimica et biophysica acta, Vol. 1251, No. 1, 16.08.1995, p. 17-22.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Moreau, S, Davies, MJ & Puppo, A 1995, 'Reaction of ferric leghemoglobin with H2O2: formation of heme-protein cross-links and dimeric species', Biochimica et biophysica acta, vol. 1251, no. 1, pp. 17-22.

APA

Moreau, S., Davies, M. J., & Puppo, A. (1995). Reaction of ferric leghemoglobin with H2O2: formation of heme-protein cross-links and dimeric species. Biochimica et biophysica acta, 1251(1), 17-22.

Vancouver

Moreau S, Davies MJ, Puppo A. Reaction of ferric leghemoglobin with H2O2: formation of heme-protein cross-links and dimeric species. Biochimica et biophysica acta. 1995 Aug 16;1251(1):17-22.

Author

Moreau, S ; Davies, M J ; Puppo, A. / Reaction of ferric leghemoglobin with H2O2 : formation of heme-protein cross-links and dimeric species. In: Biochimica et biophysica acta. 1995 ; Vol. 1251, No. 1. pp. 17-22.

Bibtex

@article{118d7d80bc414883bceb1158e6e14a95,
title = "Reaction of ferric leghemoglobin with H2O2: formation of heme-protein cross-links and dimeric species",
abstract = "Ferric leghemoglobin in the presence of H2O2 is known to give rise to protein radicals, at least one of which is centred on a tyrosine residue. These radicals are quenched by at least two processes. The first one involves an intramolecular heme-protein cross-link probably involving the tyrosine radical; this leads to the formation of a green compound with spectral characteristics differing markedly from those of ferryl and ferric leghemoglobin. This green compound cannot be reduced by dithionite or ascorbate, precluding any role for this species as an oxygen carrier. It exhibits modified EPR and pyridine haemochromogen spectra, indicating that alterations occur at the porphyrin macrocycle level. The additional compound previously described [Puppo, A., Monny, C. and Davies, M.J. (1993) Biochem. J. 289, 435-438] appears to be a mixture of ferry Lb and this green compound. The second quenching route results in the formation of intermolecular cross-links and hence dimeric forms of the protein. Ascorbate and glutathione inhibit both this intermolecular dimer formation and the formation of the intramolecular haem-protein cross-links and are likely to play a protective role in vivo.",
keywords = "Electron Spin Resonance Spectroscopy, Ferric Compounds, Hydrogen Peroxide, Leghemoglobin, Soybeans, Spectrophotometry",
author = "S Moreau and Davies, {M J} and A Puppo",
year = "1995",
month = "8",
day = "16",
language = "English",
volume = "1251",
pages = "17--22",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Reaction of ferric leghemoglobin with H2O2

T2 - formation of heme-protein cross-links and dimeric species

AU - Moreau, S

AU - Davies, M J

AU - Puppo, A

PY - 1995/8/16

Y1 - 1995/8/16

N2 - Ferric leghemoglobin in the presence of H2O2 is known to give rise to protein radicals, at least one of which is centred on a tyrosine residue. These radicals are quenched by at least two processes. The first one involves an intramolecular heme-protein cross-link probably involving the tyrosine radical; this leads to the formation of a green compound with spectral characteristics differing markedly from those of ferryl and ferric leghemoglobin. This green compound cannot be reduced by dithionite or ascorbate, precluding any role for this species as an oxygen carrier. It exhibits modified EPR and pyridine haemochromogen spectra, indicating that alterations occur at the porphyrin macrocycle level. The additional compound previously described [Puppo, A., Monny, C. and Davies, M.J. (1993) Biochem. J. 289, 435-438] appears to be a mixture of ferry Lb and this green compound. The second quenching route results in the formation of intermolecular cross-links and hence dimeric forms of the protein. Ascorbate and glutathione inhibit both this intermolecular dimer formation and the formation of the intramolecular haem-protein cross-links and are likely to play a protective role in vivo.

AB - Ferric leghemoglobin in the presence of H2O2 is known to give rise to protein radicals, at least one of which is centred on a tyrosine residue. These radicals are quenched by at least two processes. The first one involves an intramolecular heme-protein cross-link probably involving the tyrosine radical; this leads to the formation of a green compound with spectral characteristics differing markedly from those of ferryl and ferric leghemoglobin. This green compound cannot be reduced by dithionite or ascorbate, precluding any role for this species as an oxygen carrier. It exhibits modified EPR and pyridine haemochromogen spectra, indicating that alterations occur at the porphyrin macrocycle level. The additional compound previously described [Puppo, A., Monny, C. and Davies, M.J. (1993) Biochem. J. 289, 435-438] appears to be a mixture of ferry Lb and this green compound. The second quenching route results in the formation of intermolecular cross-links and hence dimeric forms of the protein. Ascorbate and glutathione inhibit both this intermolecular dimer formation and the formation of the intramolecular haem-protein cross-links and are likely to play a protective role in vivo.

KW - Electron Spin Resonance Spectroscopy

KW - Ferric Compounds

KW - Hydrogen Peroxide

KW - Leghemoglobin

KW - Soybeans

KW - Spectrophotometry

M3 - Journal article

C2 - 7647088

VL - 1251

SP - 17

EP - 22

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 1

ER -

ID: 152246913