The reactions of hydropersulfides (RSSH) with myoglobin
Copyright © 2020 Elsevier Inc. All rights reserved..
Hydropersulfides are reported to be good biological reductants, superior to thiols and akin to selenols. As such, they have been previously shown to reduce metalloproteins such as ferric myoglobin and ferric cytochrome c to their ferrous forms under conditions where little or no reduction from corresponding thiols is observed. Not surprisingly, the reduction of ferric myoglobin to ferrous myoglobin under aerobic conditions results in the generation of oxymyoglobin (dioxygen bound ferrous myoglobin). Previous studies have demonstrated that oxymyoglobin can also act as an oxidant with highly reducing species such as hydroxylamine and ascorbate. Considering the reducing properties of hydropersulfides, it is possible that they can also react with oxymyoglobin similarly to hydroxylamine or ascorbate. Herein, this reaction is examined and indeed hydropersulfides are found to react with oxymyoglobin similarly to other reducing species leading to a fleeting ferric myoglobin which is rapidly reduced to the ferrous form also by hydropersulfide.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2020 |
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Erschienen: |
2020 |
Enthalten in: |
Zur Gesamtaufnahme - volume:687 |
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Enthalten in: |
Archives of biochemistry and biophysics - 687(2020) vom: 15. Juli, Seite 108391 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Álvarez, Lucía [VerfasserIn] |
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Links: |
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Anmerkungen: |
Date Completed 02.10.2020 Date Revised 02.10.2020 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1016/j.abb.2020.108391 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM309443571 |
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520 | |a Hydropersulfides are reported to be good biological reductants, superior to thiols and akin to selenols. As such, they have been previously shown to reduce metalloproteins such as ferric myoglobin and ferric cytochrome c to their ferrous forms under conditions where little or no reduction from corresponding thiols is observed. Not surprisingly, the reduction of ferric myoglobin to ferrous myoglobin under aerobic conditions results in the generation of oxymyoglobin (dioxygen bound ferrous myoglobin). Previous studies have demonstrated that oxymyoglobin can also act as an oxidant with highly reducing species such as hydroxylamine and ascorbate. Considering the reducing properties of hydropersulfides, it is possible that they can also react with oxymyoglobin similarly to hydroxylamine or ascorbate. Herein, this reaction is examined and indeed hydropersulfides are found to react with oxymyoglobin similarly to other reducing species leading to a fleeting ferric myoglobin which is rapidly reduced to the ferrous form also by hydropersulfide | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, Non-U.S. Gov't | |
650 | 4 | |a Research Support, U.S. Gov't, Non-P.H.S. | |
650 | 4 | |a Hydrogen sulfide | |
650 | 4 | |a Hydropersulfides | |
650 | 4 | |a Myoglobin | |
650 | 4 | |a Polysulfides | |
650 | 4 | |a Sulfheme | |
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700 | 1 | |a Suarez Vega, Valeria |e verfasserin |4 aut | |
700 | 1 | |a McGinity, Christopher |e verfasserin |4 aut | |
700 | 1 | |a Khodade, Vinayak S |e verfasserin |4 aut | |
700 | 1 | |a Toscano, John P |e verfasserin |4 aut | |
700 | 1 | |a Nagy, Peter |e verfasserin |4 aut | |
700 | 1 | |a Lin, Joseph |e verfasserin |4 aut | |
700 | 1 | |a Works, Carmen |e verfasserin |4 aut | |
700 | 1 | |a Fukuto, Jon M |e verfasserin |4 aut | |
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