Ferrocyanide − a novel catalyst for oxymyoglobin oxidation by molecular oxygen
A comparative study of the rates of ferrocyanide‐catalyzed oxidation of several oxymyoglobins by molecular oxygen is reported. Oxidation of the native oxymyoglobins from sperm whale, horse and pig, as well as the chemically modified (MbO 2 ) sperm whale oxymyoglobin, with all accessible His residues...
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crwiley:10.1111/j.1742-4658.2007.06061.x 2023-12-03T10:30:46+01:00 Ferrocyanide − a novel catalyst for oxymyoglobin oxidation by molecular oxygen Postnikova, G. B. Moiseeva, S. A. Shekhovtsova, E. A. Goraev, E. V. Sivozhelezov, V. S. 2007 http://dx.doi.org/10.1111/j.1742-4658.2007.06061.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1742-4658.2007.06061.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1742-4658.2007.06061.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor The FEBS Journal volume 274, issue 20, page 5360-5369 ISSN 1742-464X 1742-4658 Cell Biology Molecular Biology Biochemistry journal-article 2007 crwiley https://doi.org/10.1111/j.1742-4658.2007.06061.x 2023-11-09T14:09:57Z A comparative study of the rates of ferrocyanide‐catalyzed oxidation of several oxymyoglobins by molecular oxygen is reported. Oxidation of the native oxymyoglobins from sperm whale, horse and pig, as well as the chemically modified (MbO 2 ) sperm whale oxymyoglobin, with all accessible His residues alkylated by sodium bromoacetate (CM‐MbO 2 ), and the mutant sperm whale oxymyoglobin [MbO 2 (His119→Asp)], was studied. The effect of pH, ionic strength and the concentration of anionic catalyst ferrocyanide, [Fe(CN) 6 ] 4– , on the oxidation rate is investigated, as well as the effect of MbO 2 complexing with redox‐inactive Zn 2+ , which forms the stable chelate complex with functional groups of His119, Lys16 and Asp122, all located nearby. The catalytic mechanism was demonstrated to involve specific [Fe(CN) 6 ] 4– binding to the protein in the His119 region, which agrees with a high local positive electrostatic potential and the presence of a cavity large enough to accommodate [Fe(CN) 6 ] 4– in that region. The protonation of the nearby His113 and especially His116 plays a very important role in the catalysis, accelerating the oxidation rate of bound [Fe(CN) 6 ] 4– by dissolved oxygen. The simultaneous occurrence of both these factors (i.e. specific binding of [Fe(CN) 6 ] 4– to the protein and its fast reoxidation by oxygen) is necessary for the efficient ferrocyanide‐catalyzed oxidation of oxymyoglobin. Article in Journal/Newspaper Sperm whale Wiley Online Library (via Crossref) The FEBS Journal 274 20 5360 5369 |
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Wiley Online Library (via Crossref) |
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English |
topic |
Cell Biology Molecular Biology Biochemistry |
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Cell Biology Molecular Biology Biochemistry Postnikova, G. B. Moiseeva, S. A. Shekhovtsova, E. A. Goraev, E. V. Sivozhelezov, V. S. Ferrocyanide − a novel catalyst for oxymyoglobin oxidation by molecular oxygen |
topic_facet |
Cell Biology Molecular Biology Biochemistry |
description |
A comparative study of the rates of ferrocyanide‐catalyzed oxidation of several oxymyoglobins by molecular oxygen is reported. Oxidation of the native oxymyoglobins from sperm whale, horse and pig, as well as the chemically modified (MbO 2 ) sperm whale oxymyoglobin, with all accessible His residues alkylated by sodium bromoacetate (CM‐MbO 2 ), and the mutant sperm whale oxymyoglobin [MbO 2 (His119→Asp)], was studied. The effect of pH, ionic strength and the concentration of anionic catalyst ferrocyanide, [Fe(CN) 6 ] 4– , on the oxidation rate is investigated, as well as the effect of MbO 2 complexing with redox‐inactive Zn 2+ , which forms the stable chelate complex with functional groups of His119, Lys16 and Asp122, all located nearby. The catalytic mechanism was demonstrated to involve specific [Fe(CN) 6 ] 4– binding to the protein in the His119 region, which agrees with a high local positive electrostatic potential and the presence of a cavity large enough to accommodate [Fe(CN) 6 ] 4– in that region. The protonation of the nearby His113 and especially His116 plays a very important role in the catalysis, accelerating the oxidation rate of bound [Fe(CN) 6 ] 4– by dissolved oxygen. The simultaneous occurrence of both these factors (i.e. specific binding of [Fe(CN) 6 ] 4– to the protein and its fast reoxidation by oxygen) is necessary for the efficient ferrocyanide‐catalyzed oxidation of oxymyoglobin. |
format |
Article in Journal/Newspaper |
author |
Postnikova, G. B. Moiseeva, S. A. Shekhovtsova, E. A. Goraev, E. V. Sivozhelezov, V. S. |
author_facet |
Postnikova, G. B. Moiseeva, S. A. Shekhovtsova, E. A. Goraev, E. V. Sivozhelezov, V. S. |
author_sort |
Postnikova, G. B. |
title |
Ferrocyanide − a novel catalyst for oxymyoglobin oxidation by molecular oxygen |
title_short |
Ferrocyanide − a novel catalyst for oxymyoglobin oxidation by molecular oxygen |
title_full |
Ferrocyanide − a novel catalyst for oxymyoglobin oxidation by molecular oxygen |
title_fullStr |
Ferrocyanide − a novel catalyst for oxymyoglobin oxidation by molecular oxygen |
title_full_unstemmed |
Ferrocyanide − a novel catalyst for oxymyoglobin oxidation by molecular oxygen |
title_sort |
ferrocyanide − a novel catalyst for oxymyoglobin oxidation by molecular oxygen |
publisher |
Wiley |
publishDate |
2007 |
url |
http://dx.doi.org/10.1111/j.1742-4658.2007.06061.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1742-4658.2007.06061.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1742-4658.2007.06061.x |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
The FEBS Journal volume 274, issue 20, page 5360-5369 ISSN 1742-464X 1742-4658 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/j.1742-4658.2007.06061.x |
container_title |
The FEBS Journal |
container_volume |
274 |
container_issue |
20 |
container_start_page |
5360 |
op_container_end_page |
5369 |
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1784256800425508864 |