AI Article Synopsis
- Persulfides like cysteine, glutathione, and N-methoxycarbonyl-penicillamine react with the ferric form of myoglobin to form either oxy-ferrous or deoxy-ferrous myoglobin, depending on aerobic or anaerobic conditions.
- Under aerobic conditions, certain persulfides react with a hypervalent form of myoglobin, resulting in intermediates like metMb and ultimately producing oxyMb.
- Experiments indicate a redox balance between ferric and ferrous heme forms and suggest that persulfides have unique redox properties similar to dihydrolipoic acid.
Article Abstract
Persulfides of cysteine (CysSSH), glutathione (GSSH) or N-methoxycarbonyl-penicillamine (NAcPenSSH) react with the ferric form of myoglobin (metMb(iii)) to yield the oxy-ferrous (oxyMb(ii)) or deoxy-ferrous (deoxyMb(ii)) forms of myoglobin under aerobic or anaerobic conditions, respectively. Under aerobic conditions, CysSSH and NAcPenSSH react with the hypervalent form of myoglobin (ferrylMb(iv)) to yield oxyMb(ii) as the final product with the formation of metMb(iii) as an intermediate. CysSSH and NAcPenSSH coordinate the ferric form of N-acetylated microperoxidase (NAcMP11(iii)) to yield the disulfanido complex NAcMP11(iii)(NAcPenSS), as shown by UV-vis and EPR spectroscopy. Experiments carried out with various NAcMP11 derivatives demonstrate a redox equilibrium between the ferric/ferrous forms of the heme and the polysulfides/persulfides couple. Our results suggest that persulfides possess uncommon redox properties, analogous to that of dihydrolipoic acid.
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| http://dx.doi.org/10.1039/c7dt01638g | DOI Listing |
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Reactions of persulfides with the heme cofactor of oxidized myoglobin and microperoxidase 11: reduction or coordination.
Dalton Trans
June 2017
UMR 8601, LCBPT, CNRS-Université Paris Descartes, Sorbonne Paris Cité, 45 rue des Sts Pères, 75006 Paris, France.
Article Synopsis
- Persulfides like cysteine, glutathione, and N-methoxycarbonyl-penicillamine react with the ferric form of myoglobin to form either oxy-ferrous or deoxy-ferrous myoglobin, depending on aerobic or anaerobic conditions.
- Under aerobic conditions, certain persulfides react with a hypervalent form of myoglobin, resulting in intermediates like metMb and ultimately producing oxyMb.
- Experiments indicate a redox balance between ferric and ferrous heme forms and suggest that persulfides have unique redox properties similar to dihydrolipoic acid.
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